메뉴 건너뛰기




Volumn 153, Issue , 2005, Pages 47-99

Molecular mechanisms of membrane polarity in renal epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 16444373095     PISSN: 03034240     EISSN: None     Source Type: Book Series    
DOI: 10.1007/s10254-004-0037-1     Document Type: Review
Times cited : (21)

References (386)
  • 1
    • 0030464473 scopus 로고    scopus 로고
    • Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion
    • Adams CL, Nelson WJ, Smith SJ (1996) Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion. J Cell Biol 135:1899-1911
    • (1996) J Cell Biol , vol.135 , pp. 1899-1911
    • Adams, C.L.1    Nelson, W.J.2    Smith, S.J.3
  • 2
    • 0032563564 scopus 로고    scopus 로고
    • Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein
    • Adams CL, Chen YT, Smith SJ, Nelson WJ (1998) Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein. J Cell Biol 142:1105-1119
    • (1998) J Cell Biol , vol.142 , pp. 1105-1119
    • Adams, C.L.1    Chen, Y.T.2    Smith, S.J.3    Nelson, W.J.4
  • 3
    • 0035494421 scopus 로고    scopus 로고
    • In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4
    • Adams ME, Mueller HA, Froehner SC (2001) In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4. J Cell Biol 155:113-122
    • (2001) J Cell Biol , vol.155 , pp. 113-122
    • Adams, M.E.1    Mueller, H.A.2    Froehner, S.C.3
  • 4
    • 13344249735 scopus 로고    scopus 로고
    • Polarized expression of GABA transporters in Madin-Darby canine kidney cells and cultured hippocampal neurons
    • Ahn J, Mundigl O, Muth TR, Rudnick G, Caplan MJ (1996) Polarized expression of GABA transporters in Madin-Darby canine kidney cells and cultured hippocampal neurons. J Biol Chem 271:6917-6924
    • (1996) J Biol Chem , vol.271 , pp. 6917-6924
    • Ahn, J.1    Mundigl, O.2    Muth, T.R.3    Rudnick, G.4    Caplan, M.J.5
  • 5
    • 0038041944 scopus 로고    scopus 로고
    • Terminal differentiation of intercalated cells: The role of hensin
    • Al-Awqati, Q (2003) Terminal differentiation of intercalated cells: The role of hensin. Annu Rev Physiol 65:567-583
    • (2003) Annu Rev Physiol , vol.65 , pp. 567-583
    • Al-Awqati, Q.1
  • 6
    • 0004183876 scopus 로고
    • cDNA cloning and sequence of MAL: A hydrophobic protein associated with human T-cell differentiation
    • Alonso MA, Weissman SM (1987) cDNA cloning and sequence of MAL: A hydrophobic protein associated with human T-cell differentiation. Proc Natl Acad Sci 84 1997-2001
    • (1987) Proc Natl Acad Sci , vol.84 , pp. 1997-2001
    • Alonso, M.A.1    Weissman, S.M.2
  • 7
    • 0030113804 scopus 로고    scopus 로고
    • Cell signalling: MAGUK magic
    • Anderson JM (1996) Cell signalling: MAGUK magic. Curr Biol 6:382-334
    • (1996) Curr Biol , vol.6 , pp. 334-382
    • Anderson, J.M.1
  • 8
    • 0242298589 scopus 로고    scopus 로고
    • The Rab 8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells
    • Ang AL, Folsch H, Koivisto UM, Pypaert M, Mellman I (2003) The Rab 8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells. J Cell Biol 163:339-350
    • (2003) J Cell Biol , vol.163 , pp. 339-350
    • Ang, A.L.1    Folsch, H.2    Koivisto, U.M.3    Pypaert, M.4    Mellman, I.5
  • 9
    • 0035009245 scopus 로고    scopus 로고
    • Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton
    • Apodaca G (2001) Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton. Traffic 2:149-159
    • (2001) Traffic , vol.2 , pp. 149-159
    • Apodaca, G.1
  • 10
    • 0028346520 scopus 로고
    • Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca G, Katz LA, Mostov KE (1994) Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J Cell Biol 125:67-86
    • (1994) J Cell Biol , vol.125 , pp. 67-86
    • Apodaca, G.1    Katz, L.A.2    Mostov, K.E.3
  • 11
    • 0029990362 scopus 로고    scopus 로고
    • Reconstitution of transcytosis in SLO-permeabilized MDCK cells: Existence of an NSF-dependent fusion mechanism with the apical surface of MDCK cells
    • Apodaca G, Cardone MH, Whiteheart SW, Dasgupta BR, Mostov KE (1996) Reconstitution of transcytosis in SLO-permeabilized MDCK cells: existence of an NSF-dependent fusion mechanism with the apical surface of MDCK cells. EMBO J 15:1471-1481
    • (1996) EMBO J , vol.15 , pp. 1471-1481
    • Apodaca, G.1    Cardone, M.H.2    Whiteheart, S.W.3    Dasgupta, B.R.4    Mostov, K.E.5
  • 12
    • 0027383316 scopus 로고
    • Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor
    • Aroeti B, Kosen PA, Kuntz ID, Cohen FE, Mostov KE (1993) Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor. J Cell Biol 123:1149-1160
    • (1993) J Cell Biol , vol.123 , pp. 1149-1160
    • Aroeti, B.1    Kosen, P.A.2    Kuntz, I.D.3    Cohen, F.E.4    Mostov, K.E.5
  • 13
    • 0032753450 scopus 로고    scopus 로고
    • Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells
    • Asakura T, Nakanishi H, Sakisaka T, Takahashi K, Mandai K, Nishimura M, Sasaki T, Takai Y (1999) Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells. Genes Cells 4:573-581
    • (1999) Genes Cells , vol.4 , pp. 573-581
    • Asakura, T.1    Nakanishi, H.2    Sakisaka, T.3    Takahashi, K.4    Mandai, K.5    Nishimura, M.6    Sasaki, T.7    Takai, Y.8
  • 14
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium
    • Bacallao R, Antony C, Dotti C, Karsenti E, Stelzer EH, Simons K (1989) The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J Cell Biol 109:2817-2832
    • (1989) J Cell Biol , vol.109 , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.H.5    Simons, K.6
  • 15
    • 0035818984 scopus 로고    scopus 로고
    • Drosophila Stardust is a partner of Crumbs in the control of epithelial cell polarity
    • Bachmann A, Schneider M, Theilenberg E, Grawe F, Knust E (2001) Drosophila Stardust is a partner of Crumbs in the control of epithelial cell polarity. Nature 414:638-643
    • (2001) Nature , vol.414 , pp. 638-643
    • Bachmann, A.1    Schneider, M.2    Theilenberg, E.3    Grawe, F.4    Knust, E.5
  • 16
    • 0345377061 scopus 로고
    • Development of cell surface polarity in the epithelial Madin-Darby canine kidney (MDCK) cell line
    • Balcarova-Stander J, Pfeiffer SE, Fuller SD, Simons K (1984) Development of cell surface polarity in the epithelial Madin-Darby canine kidney (MDCK) cell line. EMBO J 3:2687-2694
    • (1984) EMBO J , vol.3 , pp. 2687-2694
    • Balcarova-Stander, J.1    Pfeiffer, S.E.2    Fuller, S.D.3    Simons, K.4
  • 17
    • 0033543660 scopus 로고    scopus 로고
    • SNARE proteins regulate H(+)-ATPase redistribution to the apical membrane in rat renal inner medullary collecting duct cells
    • Banerjee A, Shih T, Alexander EA, Schwartz JH (1999) SNARE proteins regulate H(+)-ATPase redistribution to the apical membrane in rat renal inner medullary collecting duct cells. J Biol Chem 274:26518-26522
    • (1999) J Biol Chem , vol.274 , pp. 26518-26522
    • Banerjee, A.1    Shih, T.2    Alexander, E.A.3    Schwartz, J.H.4
  • 18
    • 0035005738 scopus 로고    scopus 로고
    • Role of SNAP-23 in trafficking of H+-ATPase in cultured inner medullary collecting duct cells
    • Banerjee A, Li G, Alexander EA, Schwartz JH (2001) Role of SNAP-23 in trafficking of H+-ATPase in cultured inner medullary collecting duct cells. Am J Physiol Cell Physiol 280:C775-C781
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Banerjee, A.1    Li, G.2    Alexander, E.A.3    Schwartz, J.H.4
  • 19
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard RJ, Morgan A, Burgoyne RD (1997) Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis. J Cell Biol 139:875-883
    • (1997) J Cell Biol , vol.139 , pp. 875-883
    • Barnard, R.J.1    Morgan, A.2    Burgoyne, R.D.3
  • 20
    • 0342327346 scopus 로고    scopus 로고
    • Cadherins, catenins and APC protein: Interplay between cytoskeletal complexes and signaling pathways
    • Barth AI, Nathke IS, Nelson WJ (1997) Cadherins, catenins and APC protein: Interplay between cytoskeletal complexes and signaling pathways. Curr Opin Cell Biol 9:683-690
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 683-690
    • Barth, A.I.1    Nathke, I.S.2    Nelson, W.J.3
  • 21
    • 0023608934 scopus 로고
    • Biogenesis of the rat hepatocyte plasma membrane in vivo: Comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation
    • Bartles JR, Feracci HM, Stieger B, Hubbard AL (1987) Biogenesis of the rat hepatocyte plasma membrane in vivo: Comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation. J Cell Biol 105:1241-1251
    • (1987) J Cell Biol , vol.105 , pp. 1241-1251
    • Bartles, J.R.1    Feracci, H.M.2    Stieger, B.3    Hubbard, A.L.4
  • 22
    • 0038158316 scopus 로고    scopus 로고
    • The role of the C terminus and na+/h+ exchanger regulatory factor in the functional expression of cystic fibrosis transmembrane conductance regulator in nonpolarized cells and epithelia
    • Benharouga M, Sharma M, So J, Haardt M, Drzymala L, Popov M, Schwapach B, Grinstein S, Du K, Lukacs GL (2003) The role of the C terminus and na+/h+ exchanger regulatory factor in the functional expression of cystic fibrosis transmembrane conductance regulator in nonpolarized cells and epithelia. J Biol Chem 278:22079-22089
    • (2003) J Biol Chem , vol.278 , pp. 22079-22089
    • Benharouga, M.1    Sharma, M.2    So, J.3    Haardt, M.4    Drzymala, L.5    Popov, M.6    Schwapach, B.7    Grinstein, S.8    Du, K.9    Lukacs, G.L.10
  • 23
    • 0024293570 scopus 로고
    • Release of putative exocytic transport vesicles from perforated MDCK cells
    • Bennett MK, Wandinger-Ness A, Simons K (1988) Release of putative exocytic transport vesicles from perforated MDCK cells. EMBO J 7:4075-4085
    • (1988) EMBO J , vol.7 , pp. 4075-4085
    • Bennett, M.K.1    Wandinger-Ness, A.2    Simons, K.3
  • 24
    • 0033606823 scopus 로고    scopus 로고
    • N-Glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells
    • Benting JH, Rietveld AG, Simons K (1999) N-Glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells. J Cell Biol 146:313-320
    • (1999) J Cell Biol , vol.146 , pp. 313-320
    • Benting, J.H.1    Rietveld, A.G.2    Simons, K.3
  • 25
    • 0033582916 scopus 로고    scopus 로고
    • Discs Lost a novel multi-PDZ domain protein, establishes and maintains epithelial polarity
    • Bhat MA, Izaddoost S, Lu Y, Cho KO, Choi KW, Bellen HJ (1999) Discs Lost a novel multi-PDZ domain protein, establishes and maintains epithelial polarity. Cell 96:833-845
    • (1999) Cell , vol.96 , pp. 833-845
    • Bhat, M.A.1    Izaddoost, S.2    Lu, Y.3    Cho, K.O.4    Choi, K.W.5    Bellen, H.J.6
  • 26
    • 0036086788 scopus 로고    scopus 로고
    • Expression of myosin VI within the early endocytic pathway in adult and developing proximal tubules
    • Biemesderfer D, Mentone SA, Mooseker M, Hasson T (2002) Expression of myosin VI within the early endocytic pathway in adult and developing proximal tubules. Am J Physiol Renal Physiol 282:F785-F794
    • (2002) Am J Physiol Renal Physiol , vol.282
    • Biemesderfer, D.1    Mentone, S.A.2    Mooseker, M.3    Hasson, T.4
  • 27
    • 0034628471 scopus 로고    scopus 로고
    • Localization of apical epithelial determinants by the basolateral PDZ protein Scribble
    • Bilder D, Perrimon N (2000) Localization of apical epithelial determinants by the basolateral PDZ protein Scribble. Nature 403:676-680
    • (2000) Nature , vol.403 , pp. 676-680
    • Bilder, D.1    Perrimon, N.2
  • 28
    • 0034617129 scopus 로고    scopus 로고
    • Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors
    • Bilder D, Li M, Perrimon N (2000) Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors. Science 289:113-116
    • (2000) Science , vol.289 , pp. 113-116
    • Bilder, D.1    Li, M.2    Perrimon, N.3
  • 29
    • 0037228253 scopus 로고    scopus 로고
    • Integrated activity of PDZ protein complexes regulates epithelial polarity
    • Bilder D, Schober M, Perrimon N (2003) Integrated activity of PDZ protein complexes regulates epithelial polarity. Nat Cell Biol 5:53-58
    • (2003) Nat Cell Biol , vol.5 , pp. 53-58
    • Bilder, D.1    Schober, M.2    Perrimon, N.3
  • 30
    • 0035158494 scopus 로고    scopus 로고
    • Adaptins: The final recount
    • Boehm M, Bonifacino JS (2001) Adaptins: The final recount. Mol Biol Cell 12:2907-2920
    • (2001) Mol Biol Cell , vol.12 , pp. 2907-2920
    • Boehm, M.1    Bonifacino, J.S.2
  • 31
    • 0026014467 scopus 로고
    • Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells
    • Boll W, Partin JS, Katz AI, Caplan MJ, Jamieson JD (1991) Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells. Proc Natl Acad Sci 88:8592-8596
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 8592-8596
    • Boll, W.1    Partin, J.S.2    Katz, A.I.3    Caplan, M.J.4    Jamieson, J.D.5
  • 33
    • 0025029828 scopus 로고
    • Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells
    • Bomsel M, Parton R, Kuznetsov SA, Schroer TA, Gruenberg J (1990) Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells. Cell 62:719-731
    • (1990) Cell , vol.62 , pp. 719-731
    • Bomsel, M.1    Parton, R.2    Kuznetsov, S.A.3    Schroer, T.A.4    Gruenberg, J.5
  • 34
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino JS, Dell'angelica EC (1999) Molecular bases for the recognition of tyrosine-based sorting signals. J Cell Biol 145:923-926
    • (1999) J Cell Biol , vol.145 , pp. 923-926
    • Bonifacino, J.S.1    Dell'angelica, E.C.2
  • 35
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino JS, Traub LM (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72:395-447
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 38
    • 0025605057 scopus 로고
    • Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells
    • Breitfeld PP, Mckinnon WC, Mostov KE (1990) Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells. J Cell Biol 111:2365-2373
    • (1990) J Cell Biol , vol.111 , pp. 2365-2373
    • Breitfeld, P.P.1    Mckinnon, W.C.2    Mostov, K.E.3
  • 39
    • 0031934911 scopus 로고    scopus 로고
    • Basolateral distribution of caveolin-1 in the kidney. Absence from H+-atpase-coated endocytic vesicles in intercalated cells
    • Breton S, Lisanti MP, Tyszkowski R, Mclaughlin M, Brown D (1998) Basolateral distribution of caveolin-1 in the kidney. Absence from H+-atpase-coated endocytic vesicles in intercalated cells. J Histochem Cytochem 46:205-214
    • (1998) J Histochem Cytochem , vol.46 , pp. 205-214
    • Breton, S.1    Lisanti, M.P.2    Tyszkowski, R.3    Mclaughlin, M.4    Brown, D.5
  • 40
    • 0034033704 scopus 로고    scopus 로고
    • Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract
    • Breton S, Nsumu NN, Galli T, Sabolic I, Smith PJ, Brown D (2000) Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract. Am J Physiol Renal Physiol 278:F717-F725
    • (2000) Am J Physiol Renal Physiol , vol.278
    • Breton, S.1    Nsumu, N.N.2    Galli, T.3    Sabolic, I.4    Smith, P.J.5    Brown, D.6
  • 41
    • 0036087084 scopus 로고    scopus 로고
    • Antigen retrieval reveals widespread basolateral expression of syntaxin 3 in renal epithelia
    • Breton S, Inoue T, Knepper MA, Brown D (2002) Antigen retrieval reveals widespread basolateral expression of syntaxin 3 in renal epithelia. Am J Physiol Renal Physiol 282:F523-F559
    • (2002) Am J Physiol Renal Physiol , vol.282
    • Breton, S.1    Inoue, T.2    Knepper, M.A.3    Brown, D.4
  • 42
    • 1942486860 scopus 로고    scopus 로고
    • The C-terminal tail of the GAT-2 GABA transporter contains a novel motif that plays a role in basolateral targeting
    • Brown A, Muth T, Caplan MJ (2004) The C-terminal tail of the GAT-2 GABA transporter contains a novel motif that plays a role in basolateral targeting. Am J Physiol Cell Physiol 286(5):C1071-1077
    • (2004) Am J Physiol Cell Physiol , vol.286 , Issue.5
    • Brown, A.1    Muth, T.2    Caplan, M.J.3
  • 43
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E (1998) Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 14:111-136
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 44
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68:533-544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 45
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown DA, Crise B, Rose JK (1989) Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science 245:1499-1501
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 46
    • 0034139848 scopus 로고    scopus 로고
    • Definition of distinct compartments in polarized Madin-Darby canine kidney (MDCK) cells for membrane-volume sorting, polarized sorting and apical recycling
    • Brown PS, Wang E, Aroeti B, Chapin SJ, Mostov KE, Dunn KW (2000) Definition of distinct compartments in polarized Madin-Darby canine kidney (MDCK) cells for membrane-volume sorting, polarized sorting and apical recycling. Traffic 1:124-140
    • (2000) Traffic , vol.1 , pp. 124-140
    • Brown, P.S.1    Wang, E.2    Aroeti, B.3    Chapin, S.J.4    Mostov, K.E.5    Dunn, K.W.6
  • 47
    • 0028290669 scopus 로고
    • Rab 5a is a common component of the apical and basolateral endocytic machinery in polarized epithelial cells
    • Bucci C, Wandinger-Ness A, Lutcke A, Chiariello M, Bruni CB, Zerial M (1994) Rab 5a is a common component of the apical and basolateral endocytic machinery in polarized epithelial cells. Proc Natl Acad Sci 91:5061-5065
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 5061-5065
    • Bucci, C.1    Wandinger-Ness, A.2    Lutcke, A.3    Chiariello, M.4    Bruni, C.B.5    Zerial, M.6
  • 48
    • 0032939346 scopus 로고    scopus 로고
    • Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton
    • Bunn RC, Jensen MA, Reed BC (1999) Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton. Mol Biol Cell 10:819-832
    • (1999) Mol Biol Cell , vol.10 , pp. 819-832
    • Bunn, R.C.1    Jensen, M.A.2    Reed, B.C.3
  • 49
    • 0032544613 scopus 로고    scopus 로고
    • A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
    • Butz S, Okamoto M, Sudhof TC (1998) A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell 94:773-782
    • (1998) Cell , vol.94 , pp. 773-782
    • Butz, S.1    Okamoto, M.2    Sudhof, T.C.3
  • 50
    • 0031823194 scopus 로고    scopus 로고
    • Rab 11a redistributes to apical secretory canaliculus during stimulation of gastric parietal cells
    • Calhoun BC, Lapierre LA, Chew CS, Goldenring JR (1998) Rab 11a redistributes to apical secretory canaliculus during stimulation of gastric parietal cells. Am J Physiol 275:C163-C170
    • (1998) Am J Physiol , vol.275
    • Calhoun, B.C.1    Lapierre, L.A.2    Chew, C.S.3    Goldenring, J.R.4
  • 51
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor
    • Cao TT, Deacon HW, Reczek D, Bretscher A, Von Zastrow M (1999) A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature 401:286-290
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    Von Zastrow, M.5
  • 52
    • 33751339795 scopus 로고    scopus 로고
    • Membrane polarity in epithelial cells: Protein sorting and establishment of polarized domains
    • Caplan MJ (1997) Membrane polarity in epithelial cells: Protein sorting and establishment of polarized domains. Am J Physiol 272:F425-429
    • (1997) Am J Physiol , vol.272
    • Caplan, M.J.1
  • 53
    • 0023050175 scopus 로고
    • Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes
    • Caplan MJ, Anderson HC, Palade GE, Jamieson JD (1986) Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes. Cell 46(4):623-631
    • (1986) Cell , vol.46 , Issue.4 , pp. 623-631
    • Caplan, M.J.1    Anderson, H.C.2    Palade, G.E.3    Jamieson, J.D.4
  • 55
    • 0025766194 scopus 로고
    • An autonomous signal for basolateral sorting in the cytoplasmic domain of the polymeric immunoglobulin receptor
    • Casanova JE, Apodaca G, Mostov KE (1991) An autonomous signal for basolateral sorting in the cytoplasmic domain of the polymeric immunoglobulin receptor. Cell 66:65-75
    • (1991) Cell , vol.66 , pp. 65-75
    • Casanova, J.E.1    Apodaca, G.2    Mostov, K.E.3
  • 57
    • 0031918158 scopus 로고    scopus 로고
    • Role of tight junctions in establishing and maintaining cell polarity
    • Cereijido M, Valdes J, Shoshani L, Contreras RG (1998) Role of tight junctions in establishing and maintaining cell polarity. Annu Rev Physiol 60:161-177
    • (1998) Annu Rev Physiol , vol.60 , pp. 161-177
    • Cereijido, M.1    Valdes, J.2    Shoshani, L.3    Contreras, R.G.4
  • 58
    • 0033825953 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions. I. Biogenesis of tight junctions and epithelial polarity
    • Cereijido M, Shoshani L, Contreras RG (2000) Molecular physiology and pathophysiology of tight junctions. I. Biogenesis of tight junctions and epithelial polarity. Am J Physiol Gastrointest Liver Physiol 279:G477-G482
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279
    • Cereijido, M.1    Shoshani, L.2    Contreras, R.G.3
  • 59
    • 0034252898 scopus 로고    scopus 로고
    • ADPKD: A human disease altering Golgi function and basolateral exocytosis in renal epithelia
    • Charron AJ, Bacallao RL, Wandinger-Ness A (2000) ADPKD: A human disease altering Golgi function and basolateral exocytosis in renal epithelia. Traffic 1:675-686
    • (2000) Traffic , vol.1 , pp. 675-686
    • Charron, A.J.1    Bacallao, R.L.2    Wandinger-Ness, A.3
  • 62
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/MAL a lipid raft-associated protein, is involved in apical transport in MDCK cells
    • Cheong KH, Zacchetti D, Schneeberger EE, Simons K (1999) VIP17/MAL a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc Natl Acad Sci 96:6241-6248
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 6241-6248
    • Cheong, K.H.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 64
    • 0033580299 scopus 로고    scopus 로고
    • The Rab 5 effector EEA1 is a core component of endosome docking
    • Christoforidis S, Mcbride HM, Burgoyne RD, Zerial M (1999) The Rab 5 effector EEA1 is a core component of endosome docking. Nature 397:621-625
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    Mcbride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 65
    • 0032494121 scopus 로고    scopus 로고
    • The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells
    • Chuang JZ, Sung CH (1998) The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells. J Cell Biol 142:1245-1556
    • (1998) J Cell Biol , vol.142 , pp. 1245-1556
    • Chuang, J.Z.1    Sung, C.H.2
  • 66
    • 0032514259 scopus 로고    scopus 로고
    • Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
    • [published erratum appears in J Cell Biol 1998 Aug 24;142(4):following 1156]
    • Cohen AR, Woods DF, Marfatia SM, Walther Z, Chishti AH, Anderson JM, Wood DFW (1998) Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells [published erratum appears in J Cell Biol 1998 Aug 24;142(4):fOllowing 1156]. J Cell Biol 142:129-138
    • (1998) J Cell Biol , vol.142 , pp. 129-138
    • Cohen, A.R.1    Woods, D.F.2    Marfatia, S.M.3    Walther, Z.4    Chishti, A.H.5    Anderson, J.M.6    Wood, D.F.W.7
  • 67
    • 0031960011 scopus 로고    scopus 로고
    • Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
    • Daniels DL, Cohen AR, Anderson JM, Brunger AT (1998) Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition. Nat Struct Biol 5:317-325
    • (1998) Nat Struct Biol , vol.5 , pp. 317-325
    • Daniels, D.L.1    Cohen, A.R.2    Anderson, J.M.3    Brunger, A.T.4
  • 70
    • 0032875135 scopus 로고    scopus 로고
    • Expression of rab11a N124I in gastric parietal cells inhibits stimulatory recruitment of the H+-K+-ATPase
    • Duman JG, Tyagarajan K, Kolsi MS, Moore HP, Forte JG (1999) Expression of rab11a N124I in gastric parietal cells inhibits stimulatory recruitment of the H+-K+-ATPase. Am J Physiol 277:C361-C372
    • (1999) Am J Physiol , vol.277
    • Duman, J.G.1    Tyagarajan, K.2    Kolsi, M.S.3    Moore, H.P.4    Forte, J.G.5
  • 71
    • 0034695917 scopus 로고    scopus 로고
    • A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase
    • Dunbar LA, Aronson P, Caplan MJ (2000) A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase. J Cell Biol 148:769-778
    • (2000) J Cell Biol , vol.148 , pp. 769-778
    • Dunbar, L.A.1    Aronson, P.2    Caplan, M.J.3
  • 72
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn KW, Mcgraw TE, Maxfield FR (1989) Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J Cell Biol 109:3303-3314
    • (1989) J Cell Biol , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    Mcgraw, T.E.2    Maxfield, F.R.3
  • 74
    • 0022827314 scopus 로고
    • Cell-matrix interactions and cell adhesion during development
    • Ekblom P, Vestweber D, Kemler R (1986) Cell-matrix interactions and cell adhesion during development. Annu Rev Cell Dev Biol 2:27-47
    • (1986) Annu Rev Cell Dev Biol , vol.2 , pp. 27-47
    • Ekblom, P.1    Vestweber, D.2    Kemler, R.3
  • 75
    • 0018942424 scopus 로고
    • A biochemical dissection of the functional polarity of the plasma membrane of the hepatocyte
    • Evans WH (1980) A biochemical dissection of the functional polarity of the plasma membrane of the hepatocyte. Biochim Biophys Acta 604:27-64
    • (1980) Biochim Biophys Acta , vol.604 , pp. 27-64
    • Evans, W.H.1
  • 76
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R (1998) Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci 95:15781-15786
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 77
    • 0033120592 scopus 로고    scopus 로고
    • A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface
    • Fernandez-Larrea J, Merlos-Suarez A, Urena JM, Baselga J, Arribas J (1999) A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface. Mol Cell 3:423-433
    • (1999) Mol Cell , vol.3 , pp. 423-433
    • Fernandez-Larrea, J.1    Merlos-Suarez, A.2    Urena, J.M.3    Baselga, J.4    Arribas, J.5
  • 79
    • 0028921025 scopus 로고
    • Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane
    • Fiedler K, Lafont F, Parton RG, Simons K (1995) Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane. J Cell Biol 128:1043-1053
    • (1995) J Cell Biol , vol.128 , pp. 1043-1053
    • Fiedler, K.1    Lafont, F.2    Parton, R.G.3    Simons, K.4
  • 80
    • 0032548828 scopus 로고    scopus 로고
    • Sec 3p is a spatial landmark for polarized secretion in budding yeast
    • Finger FP, Hughes TE, Novick P (1998) Sec 3p is a spatial landmark for polarized secretion in budding yeast. Cell 92:559-571
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.P.1    Hughes, T.E.2    Novick, P.3
  • 81
    • 0033179936 scopus 로고    scopus 로고
    • Generation and maintenance of neuronal polarity: Mechanisms of transport and targeting
    • Foletti DL, Prekeris R, Scheller RH (1999) Generation and maintenance of neuronal polarity: Mechanisms of transport and targeting. Neuron 23:641-644
    • (1999) Neuron , vol.23 , pp. 641-644
    • Foletti, D.L.1    Prekeris, R.2    Scheller, R.H.3
  • 82
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Folsch H, Ohno H, Bonifacino JS, Mellman I (1999) A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99:189-198
    • (1999) Cell , vol.99 , pp. 189-198
    • Folsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 83
    • 0035809211 scopus 로고    scopus 로고
    • Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells
    • Folsch H, Pypaert M, Schu P, Mellman I (2001) Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. J Cell Biol 152:595-606
    • (2001) J Cell Biol , vol.152 , pp. 595-606
    • Folsch, H.1    Pypaert, M.2    Schu, P.3    Mellman, I.4
  • 84
    • 0242266915 scopus 로고    scopus 로고
    • The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains
    • Folsch H, Pypaert M, Maday S, Pelletier L, Mellman I (2003) The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. J Cell Biol 163:351-362
    • (2003) J Cell Biol , vol.163 , pp. 351-362
    • Folsch, H.1    Pypaert, M.2    Maday, S.3    Pelletier, L.4    Mellman, I.5
  • 86
    • 0028948698 scopus 로고
    • Vesicle fusion proteins in rat inner medullary collecting duct and amphibian bladder
    • Franki N, Macaluso F, Gao Y, Hays RM (1995) Vesicle fusion proteins in rat inner medullary collecting duct and amphibian bladder. Am J Physiol 268:C792-C797
    • (1995) Am J Physiol , vol.268
    • Franki, N.1    Macaluso, F.2    Gao, Y.3    Hays, R.M.4
  • 89
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • Galli T, Zahraoui A, Vaidyanathan VV, Raposo G, Tian JM, Karin M, Niemann H, Louvard D (1998) A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol Biol Cell 9:1437-1438
    • (1998) Mol Biol Cell , vol.9 , pp. 1437-1438
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3    Raposo, G.4    Tian, J.M.5    Karin, M.6    Niemann, H.7    Louvard, D.8
  • 90
    • 0036045770 scopus 로고    scopus 로고
    • The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane
    • Gan Y, Mcgraw TE, Rodriguez-Boulan E (2002) The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Nat Cell Biol 4:605-609
    • (2002) Nat Cell Biol , vol.4 , pp. 605-609
    • Gan, Y.1    Mcgraw, T.E.2    Rodriguez-Boulan, E.3
  • 91
    • 0027380624 scopus 로고
    • Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor
    • Geffen I, Fuhrer C, Leitinger B, Weiss M, Huggel K, Griffiths G, Spiess M (1993) Related signals for endocytosis and basolateral sorting of the asialoglycoprotein receptor. J Biol Chem 268:20772-20777
    • (1993) J Biol Chem , vol.268 , pp. 20772-20777
    • Geffen, I.1    Fuhrer, C.2    Leitinger, B.3    Weiss, M.4    Huggel, K.5    Griffiths, G.6    Spiess, M.7
  • 93
    • 0027160730 scopus 로고
    • Identification of a small GTP-binding protein, Rab 25, expressed in the gastrointestinal mucosa, kidney, and lung
    • Goldenring JR, Shen KR, Vaughan HD, Modlin IM (1993) Identification of a small GTP-binding protein, Rab 25, expressed in the gastrointestinal mucosa, kidney, and lung. J Biol Chem 268:18419-18422
    • (1993) J Biol Chem , vol.268 , pp. 18419-18422
    • Goldenring, J.R.1    Shen, K.R.2    Vaughan, H.D.3    Modlin, I.M.4
  • 95
    • 0029978023 scopus 로고    scopus 로고
    • Clustering membrane proteins: It's all coming together with the PSD-95/ SAP90 protein family
    • [Review] [20 refs]
    • Gomperts SN (1996) Clustering membrane proteins: It's all coming together with the PSD-95/SAP90 protein family. [Review] [20 refs]. Cell 84:659-662
    • (1996) Cell , vol.84 , pp. 659-662
    • Gomperts, S.N.1
  • 96
    • 0028955867 scopus 로고
    • Biotinylation and assessment of membrane polarity: Caveats and methodological concerns
    • Gottardi CJ, Dunbar LA, Caplan MJ (1995) Biotinylation and assessment of membrane polarity: Caveats and methodological concerns. Am J Physiol 268:F285-F295
    • (1995) Am J Physiol , vol.268
    • Gottardi, C.J.1    Dunbar, L.A.2    Caplan, M.J.3
  • 97
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb TA, Ivanov IE, Adesnik M, Sabatini DD (1993) Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J Cell Biol 120:695-710
    • (1993) J Cell Biol , vol.120 , pp. 695-710
    • Gottlieb, T.A.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 98
    • 33748782944 scopus 로고    scopus 로고
    • Functional involvement of the SNARE machinery in cAMP induced AQP-2 targeting to the apical membrane in renal Epithelilia cells
    • (abstract)
    • Gouraud S, Laera A, Calamita G, Rossetto O, Montecucco C, Rosenthal W, Svelto M, Valenti G (2001) Functional involvement of the SNARE machinery in cAMP induced AQP-2 targeting to the apical membrane in renal Epithelilia cells. J Am Soc Nephrol12:A0302 (abstract)
    • (2001) J Am Soc Nephrol , vol.12
    • Gouraud, S.1    Laera, A.2    Calamita, G.3    Rossetto, O.4    Montecucco, C.5    Rosenthal, W.6    Svelto, M.7    Valenti, G.8
  • 100
    • 0029963058 scopus 로고    scopus 로고
    • The Drosophila genes crumbs and stardust are involved in the biogenesis of adherens junctions
    • Grawe F, Wodarz A, Lee B, Knust E, Skaer H (1996) The Drosophila genes crumbs and stardust are involved in the biogenesis of adherens junctions. Development 122:951-999
    • (1996) Development , vol.122 , pp. 951-999
    • Grawe, F.1    Wodarz, A.2    Lee, B.3    Knust, E.4    Skaer, H.5
  • 101
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane
    • Griffiths G, Pfeiffer S, Simons K, Matlin K (1985) Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J Cell Biol 101:949-964
    • (1985) J Cell Biol , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 102
    • 0031891269 scopus 로고    scopus 로고
    • Apiconuclear organization of microtubules does not specify protein delivery from the trans-Golgi network to different membrane domains in polarized epithelial cells
    • Grindstaff KK, Bacallao RL, Nelson WJ (1998a) Apiconuclear organization of microtubules does not specify protein delivery from the trans-Golgi network to different membrane domains in polarized epithelial cells. Mol Biol Cell 9:685-699
    • (1998) Mol Biol Cell , vol.9 , pp. 685-699
    • Grindstaff, K.K.1    Bacallao, R.L.2    Nelson, W.J.3
  • 103
    • 0032577562 scopus 로고    scopus 로고
    • Sec 6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff KK, Yeaman C, Anandasabapathy N, Hsu SC, Rodriguez-Boulan E, Scheller RH, Nelson WJ (1998b) Sec 6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93:731-740
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Anandasabapathy, N.3    Hsu, S.C.4    Rodriguez-Boulan, E.5    Scheller, R.H.6    Nelson, W.J.7
  • 104
    • 0035661621 scopus 로고    scopus 로고
    • The NH(2)-terminus of Norepinephrine transporter contains a basolateral localization signal for epithelial cells
    • Gu HH, Wu X, Giros B, Caron MG, Caplan MJ, Rudnick G (2001) The NH(2)-terminus of Norepinephrine transporter contains a basolateral localization signal for epithelial cells. Mol Biol Cell 12:3797-3807
    • (2001) Mol Biol Cell , vol.12 , pp. 3797-3807
    • Gu, H.H.1    Wu, X.2    Giros, B.3    Caron, M.G.4    Caplan, M.J.5    Rudnick, G.6
  • 105
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec 4p, targeting secretory vesicles to sites of exocytosis
    • Guo W, Roth D, Walch-Solimena C, Novick P (1999) The exocyst is an effector for Sec 4p, targeting secretory vesicles to sites of exocytosis. EMBO J 18:1071-1080
    • (1999) EMBO J , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 107
    • 0037184989 scopus 로고    scopus 로고
    • Rab 11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling
    • Hales CM, Vaerman JP, Goldenring JR (2002) Rab 11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling. J Biol Chem 277:50415-50421
    • (2002) J Biol Chem , vol.277 , pp. 50415-50421
    • Hales, C.M.1    Vaerman, J.P.2    Goldenring, J.R.3
  • 108
    • 0031754514 scopus 로고    scopus 로고
    • Microtubule-dependent vesicle transport: Modulation of channel and transporter activity in liver and kidney
    • Hamm-Alvarez SF, Sheetz MP (1998) Microtubule-dependent vesicle transport: Modulation of channel and transporter activity in liver and kidney. Physiol Rev 78:1109-1209
    • (1998) Physiol Rev , vol.78 , pp. 1109-1209
    • Hamm-Alvarez, S.F.1    Sheetz, M.P.2
  • 109
    • 0036468368 scopus 로고    scopus 로고
    • Rabs grab motors: Defining the connections between Rab GTPases and motor proteins
    • Hammer JA, Wu XS (2002) Rabs grab motors: Defining the connections between Rab GTPases and motor proteins. Curr Opin Cell Biol 14:69-75
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 69-75
    • Hammer, J.A.1    Wu, X.S.2
  • 110
    • 0029894832 scopus 로고    scopus 로고
    • Traffic, polarity, and detergent solubility of a glycosylphosphatidylinositol-anchored protein after LDL-deprivation of MDCK cells
    • Hannan LA, Edidin M (1996) Traffic, polarity, and detergent solubility of a glycosylphosphatidylinositol-anchored protein after LDL-deprivation of MDCK cells. J Cell Biol 133:1265-1276
    • (1996) J Cell Biol , vol.133 , pp. 1265-1276
    • Hannan, L.A.1    Edidin, M.2
  • 111
    • 0037013290 scopus 로고    scopus 로고
    • Involvement of VIP36 in intracellular transport and secretion of glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells
    • Hara-Kuge S, Ohkura T, Ideo H, Shimada O, Atsumi S, Yamashita K (2002) Involvement of VIP36 in intracellular transport and secretion of glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells. J Biol Chem 277:16332-16339
    • (2002) J Biol Chem , vol.277 , pp. 16332-16339
    • Hara-Kuge, S.1    Ohkura, T.2    Ideo, H.3    Shimada, O.4    Atsumi, S.5    Yamashita, K.6
  • 112
    • 0035918517 scopus 로고    scopus 로고
    • Energetic determinants of internal motif recognition by PDZ domains
    • Harris BZ, Hillier BJ, Lim WA (2001) Energetic determinants of internal motif recognition by PDZ domains. Biochim Biophys Acta 40:5921-5930
    • (2001) Biochim Biophys Acta , vol.40 , pp. 5921-5930
    • Harris, B.Z.1    Hillier, B.J.2    Lim, W.A.3
  • 113
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata Y, Slaughter CA, Sudhof TC (1993) Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366:347-351
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Sudhof, T.C.3
  • 114
    • 0034916522 scopus 로고    scopus 로고
    • Molecular determinants for apical expression and regulatory membrane retrieval of the type IIa Na/Pi cotransporter
    • Hernando N, Karim-Jimenez Z, Biber J, Murer H (2001) Molecular determinants for apical expression and regulatory membrane retrieval of the type IIa Na/Pi cotransporter. Kidney Int 60:431-435
    • (2001) Kidney Int , vol.60 , pp. 431-435
    • Hernando, N.1    Karim-Jimenez, Z.2    Biber, J.3    Murer, H.4
  • 116
    • 0021251890 scopus 로고
    • Studies on the development and maintenance of epithelial cell surface polarity with monoclonal antibodies
    • Herzlinger DA, Ojakian GK (1984) Studies on the development and maintenance of epithelial cell surface polarity with monoclonal antibodies. J Cell Biol 98:1777-1787
    • (1984) J Cell Biol , vol.98 , pp. 1777-1787
    • Herzlinger, D.A.1    Ojakian, G.K.2
  • 117
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • Hillier BJ, Christopherson KS, Prehoda KE, Bredt DS, Lim WA (1999) Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science 284:812-815
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 120
    • 0032904433 scopus 로고    scopus 로고
    • Targeting vesicles to specific sites on the plasma membrane: The role of the sec6/8 complex
    • Hsu SC, Hazuka CD, Foletti DL, Scheller RH (1999) Targeting vesicles to specific sites on the plasma membrane: The role of the sec6/8 complex. Trends Cell Biol 9:150-153
    • (1999) Trends Cell Biol , vol.9 , pp. 150-153
    • Hsu, S.C.1    Hazuka, C.D.2    Foletti, D.L.3    Scheller, R.H.4
  • 121
    • 0027517448 scopus 로고
    • Rab 8 a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane
    • Huber LA, Pimplikar S, Parton RG, Virta H, Zerial M, Simons K (1993) Rab 8 a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J Cell Biol 123:35-45
    • (1993) J Cell Biol , vol.123 , pp. 35-45
    • Huber, L.A.1    Pimplikar, S.2    Parton, R.G.3    Virta, H.4    Zerial, M.5    Simons, K.6
  • 123
    • 0025173762 scopus 로고
    • Endocytic pathways in polarized Caco-2 cells: Identification of an endosomal compartment accessible from both apical and basolateral surfaces
    • Hughson EJ, Hopkins CR (1990) Endocytic pathways in polarized Caco-2 cells: Identification of an endosomal compartment accessible from both apical and basolateral surfaces. J Cell Biol 110:337-348
    • (1990) J Cell Biol , vol.110 , pp. 337-348
    • Hughson, E.J.1    Hopkins, C.R.2
  • 124
    • 0017052382 scopus 로고
    • The origin and characteristics of a pig kidney cell strain, LLC-PK
    • Hull RN, Cherry WR, Weaver GW (1976) The origin and characteristics of a pig kidney cell strain, LLC-PK. In Vitro 12:670-677
    • (1976) In Vitro , vol.12 , pp. 670-677
    • Hull, R.N.1    Cherry, W.R.2    Weaver, G.W.3
  • 125
    • 0029962955 scopus 로고    scopus 로고
    • PSD-95 is associated with the postsynaptic density and not with the presynaptic membrane at forebrain synapses
    • Hunt CA, Schenker LJ, Kennedy MB (1996) PSD-95 is associated with the postsynaptic density and not with the presynaptic membrane at forebrain synapses. J Neurosci 16:1380-1388
    • (1996) J Neurosci , vol.16 , pp. 1380-1388
    • Hunt, C.A.1    Schenker, L.J.2    Kennedy, M.B.3
  • 126
    • 0028200044 scopus 로고
    • A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells
    • Hunziker W, Fumey C (1994) A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells. EMBO J 13:2963-2967
    • (1994) EMBO J , vol.13 , pp. 2963-2967
    • Hunziker, W.1    Fumey, C.2
  • 127
    • 0032547083 scopus 로고    scopus 로고
    • Rab 17 localizes to recycling endosomes and regulates receptor-mediated transcytosis in epithelial cells
    • Hunziker W, Peters PJ (1998) Rab 17 localizes to recycling endosomes and regulates receptor-mediated transcytosis in epithelial cells. J Biol Chem 273:15734-15741
    • (1998) J Biol Chem , vol.273 , pp. 15734-15741
    • Hunziker, W.1    Peters, P.J.2
  • 128
    • 0037319350 scopus 로고    scopus 로고
    • Direct interaction of two polarity complexes implicated in epithelial tight junction assembly
    • Hurd TW, Gao L, Roh MH, Macara IG, Margolis B (2003) Direct interaction of two polarity complexes implicated in epithelial tight junction assembly. Nat Cell Biol 5:137-142
    • (2003) Nat Cell Biol , vol.5 , pp. 137-142
    • Hurd, T.W.1    Gao, L.2    Roh, M.H.3    Macara, I.G.4    Margolis, B.5
  • 130
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen E (2001) Roles of lipid rafts in membrane transport. Curr Opin Cell Biol 13:470-477
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 131
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen E, Tagaya M, Ullrich O, Montecucco C, Simons K (1995) Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell 81:571-580
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 133
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions
    • Itoh M, Sasaki H, Furuse M, Ozaki H, Kita T, Tsukita S (2001) Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions. J Cell Biol 154:491-497
    • (2001) J Cell Biol , vol.154 , pp. 491-497
    • Itoh, M.1    Sasaki, H.2    Furuse, M.3    Ozaki, H.4    Kita, T.5    Tsukita, S.6
  • 134
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi Y, Hirose T, Tamai Y, Hirai S, Nagashima Y, Fujimoto T, Tabuse Y, Kemphues KJ, Ohno S (1998) An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J Cell Biol 143:95-106
    • (1998) J Cell Biol , vol.143 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.4    Nagashima, Y.5    Fujimoto, T.6    Tabuse, Y.7    Kemphues, K.J.8    Ohno, S.9
  • 135
    • 0034008665 scopus 로고    scopus 로고
    • Structural determinants required for apical sorting of an intestinal brush-border membrane protein
    • Jacob R, Alfalah M, Grunberg J, Obendorf M, Naim HY (2000) Structural determinants required for apical sorting of an intestinal brush-border membrane protein. J Biol Chem 275:6566-6572
    • (2000) J Biol Chem , vol.275 , pp. 6566-6572
    • Jacob, R.1    Alfalah, M.2    Grunberg, J.3    Obendorf, M.4    Naim, H.Y.5
  • 136
    • 0037380088 scopus 로고    scopus 로고
    • Distinct cytoskeletal tracks direct individual vesicle populations to the apical membrane of epithelial cells
    • Jacob R, Heine M, Alfalah M, Naim HY (2003) Distinct cytoskeletal tracks direct individual vesicle populations to the apical membrane of epithelial cells. Curr Biol 13:607-612
    • (2003) Curr Biol , vol.13 , pp. 607-612
    • Jacob, R.1    Heine, M.2    Alfalah, M.3    Naim, H.Y.4
  • 138
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R, Sudhof TC (1999) Membrane fusion and exocytosis. Annu Rev Biochem 68:863-911
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 139
    • 0028287035 scopus 로고
    • Molecular characterization and tissue distribution of ZO-2 a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein
    • Jesaitis LA, Goodenough DA (1994) Molecular characterization and tissue distribution of ZO-2 a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein. J Cell Biol 124:949-961
    • (1994) J Cell Biol , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 140
    • 0028902964 scopus 로고
    • Rat kidney papilla contains abundant synaptobrevin protein that participates in the fusion of antidiuretic hormone-regulated water channel-containing endosomes in vitro
    • Jo I, Harris HW, Amendt-Raduege AM, Majewski RR, Hammond TG (1995) Rat kidney papilla contains abundant synaptobrevin protein that participates in the fusion of antidiuretic hormone-regulated water channel-containing endosomes in vitro. Proc Natl Acad Sci 92:1876-1880
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 1876-1880
    • Jo, I.1    Harris, H.W.2    Amendt-Raduege, A.M.3    Majewski, R.R.4    Hammond, T.G.5
  • 141
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty G, Petersen C, Gao L, Macara IG (2000) The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol 2:531-559
    • (2000) Nat Cell Biol , vol.2 , pp. 531-559
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.4
  • 142
    • 0033790539 scopus 로고    scopus 로고
    • The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1
    • Johansson A, Driessens M, Aspenstrom P (2000) The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J Cell Sci 113:3267-3275
    • (2000) J Cell Sci , vol.113 , pp. 3267-3275
    • Johansson, A.1    Driessens, M.2    Aspenstrom, P.3
  • 143
    • 0032514214 scopus 로고    scopus 로고
    • Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity
    • Jou TS, Nelson WJ (1998) Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity. J Cell Biol 142:85-100
    • (1998) J Cell Biol , vol.142 , pp. 85-100
    • Jou, T.S.1    Nelson, W.J.2
  • 144
    • 0029040123 scopus 로고
    • Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex
    • Jou TS, Stewart DB, Stappert J, Nelson WJ, Marrs JA (1995) Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex. Proc Natl Acad Sci 92:5067-5071
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 5067-5071
    • Jou, T.S.1    Stewart, D.B.2    Stappert, J.3    Nelson, W.J.4    Marrs, J.A.5
  • 145
    • 0345593814 scopus 로고    scopus 로고
    • A PDZ-containing scaffold related to the dystrophin complex at the basolateral membrane of epithelial cells
    • Kachinsky AM, Froehner SC, Milgram SL (1999) A PDZ-containing scaffold related to the dystrophin complex at the basolateral membrane of epithelial cells. J Cell Biol 145:391-402
    • (1999) J Cell Biol , vol.145 , pp. 391-402
    • Kachinsky, A.M.1    Froehner, S.C.2    Milgram, S.L.3
  • 146
    • 0032544565 scopus 로고    scopus 로고
    • The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells
    • Kaech SM, Whitfield CW, Kim SK (1998) The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells. Cell 94:761-771
    • (1998) Cell , vol.94 , pp. 761-771
    • Kaech, S.M.1    Whitfield, C.W.2    Kim, S.K.3
  • 148
    • 0034859579 scopus 로고    scopus 로고
    • Molecular determinants for apical expression of the renal type IIa Na+/ Pi-cotransporter
    • Karim-Jimenez Z, Hernando N, Biber J, Murer H (2001) Molecular determinants for apical expression of the renal type IIa Na+/ Pi-cotransporter. Pflugers Arch Eur J Physiol 442:782-790
    • (2001) Pflugers Arch Eur J Physiol , vol.442 , pp. 782-790
    • Karim-Jimenez, Z.1    Hernando, N.2    Biber, J.3    Murer, H.4
  • 149
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller P, Simons K (1998) Cholesterol is required for surface transport of influenza virus hemagglutinin. J Cell Biol 140:1357-1367
    • (1998) J Cell Biol , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 150
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • Keller P, Toomre D, Diaz E, White J, Simons K (2001) Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat Cell Biol 3:140-149
    • (2001) Nat Cell Biol , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Diaz, E.3    White, J.4    Simons, K.5
  • 151
    • 0034640089 scopus 로고    scopus 로고
    • PARsing embryonic polarity
    • Kemphues K (2000) PARsing embryonic polarity. Cell 101:345-348
    • (2000) Cell , vol.101 , pp. 345-348
    • Kemphues, K.1
  • 152
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
    • Kim E, Niethammer M, Rothschild A, Jan YN, Sheng M (1995) Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases. Nature 378:85-88
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5
  • 153
    • 0034711219 scopus 로고    scopus 로고
    • E-cadherin-mediated cell-cell attachment activates Cdc42
    • Kim SH, Li Z, Sacks DB (2000) E-cadherin-mediated cell-cell attachment activates Cdc42. J Biol Chem 275:36999-37005
    • (2000) J Biol Chem , vol.275 , pp. 36999-37005
    • Kim, S.H.1    Li, Z.2    Sacks, D.B.3
  • 154
    • 0023709019 scopus 로고
    • Role of laminin A chain in the development of epithelial cell polarity
    • Klein G, Langegger M, Timpl R, Ekblom P (1988) Role of laminin A chain in the development of epithelial cell polarity. Cell 55:331-341
    • (1988) Cell , vol.55 , pp. 331-341
    • Klein, G.1    Langegger, M.2    Timpl, R.3    Ekblom, P.4
  • 155
    • 0029024637 scopus 로고
    • Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells
    • Knight A, Hughson E, Hopkins CR, Cutler DF (1995) Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells. Mol Biol Cell 6:597-610
    • (1995) Mol Biol Cell , vol.6 , pp. 597-610
    • Knight, A.1    Hughson, E.2    Hopkins, C.R.3    Cutler, D.F.4
  • 156
    • 0037032804 scopus 로고    scopus 로고
    • Composition and formation of intercellular junctions in epithelial cells
    • Knust E, Bossinger O (2002) Composition and formation of intercellular junctions in epithelial cells. Science 298:1955-1959
    • (2002) Science , vol.298 , pp. 1955-1959
    • Knust, E.1    Bossinger, O.2
  • 157
    • 0027872373 scopus 로고
    • Crumbs and stardust, two genes of Drosophila required for the development of epithelial cell polarity
    • Knust E, Tepass U, Wodarz A (1993) crumbs and stardust, two genes of Drosophila required for the development of epithelial cell polarity. Development (Suppl):261-280
    • (1993) Development , Issue.SUPPL. , pp. 261-280
    • Knust, E.1    Tepass, U.2    Wodarz, A.3
  • 158
    • 0023954085 scopus 로고
    • Colocalization and coprecipitation of ankyrin and Na+,K+-ATPase in kidney epithelial cells
    • Koob R, Zimmermann M, Schoner W, Drenckhahn D (1988) Colocalization and coprecipitation of ankyrin and Na+,K+-ATPase in kidney epithelial cells. Eur J Cell Biol 45:230-237
    • (1988) Eur J Cell Biol , vol.45 , pp. 230-237
    • Koob, R.1    Zimmermann, M.2    Schoner, W.3    Drenckhahn, D.4
  • 159
    • 0026908304 scopus 로고
    • Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins
    • Kreis TE (1992) Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins. Curr Opin Cell Biol 4:609-615
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 609-615
    • Kreis, T.E.1
  • 162
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski R, Hall A, Mellman I (1999) Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat Cell Biol 1:8-13
    • (1999) Nat Cell Biol , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 163
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu A, Avalos RT, Sanderson CM, Nayak DP (1996) Transmembrane domain of influenza virus neuraminidase a type II protein, possesses an apical sorting signal in polarized MDCK cells. J Virol 70:6508-6515
    • (1996) J Virol , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 164
    • 0028136433 scopus 로고
    • HVEM tomography of the trans-Golgi network: Structural insights and identification of a lace-like vesicle coat
    • Ladinsky MS, Kremer JR, Furcinitti PS, Mcintosh JR, Howell KE (1994) HVEM tomography of the trans-Golgi network: Structural insights and identification of a lace-like vesicle coat. J Cell Biol 127:29-38
    • (1994) J Cell Biol , vol.127 , pp. 29-38
    • Ladinsky, M.S.1    Kremer, J.R.2    Furcinitti, P.S.3    Mcintosh, J.R.4    Howell, K.E.5
  • 166
    • 0036678493 scopus 로고    scopus 로고
    • Structure of the Golgi and distribution of reporter molecules at 20 degrees C reveals the complexity of the exit compartments
    • Ladinsky MS, Wu CC, Mcintosh S, Mcintosh JR, Howell KE (2002) Structure of the Golgi and distribution of reporter molecules at 20 degrees C reveals the complexity of the exit compartments. Mol Biol Cell 13:2810-2825
    • (2002) Mol Biol Cell , vol.13 , pp. 2810-2825
    • Ladinsky, M.S.1    Wu, C.C.2    Mcintosh, S.3    Mcintosh, J.R.4    Howell, K.E.5
  • 167
    • 0028595709 scopus 로고
    • Involvement of microtubule motors in basolateral and apical transport in kidney cells
    • Lafont F, Burkhardt JK, Simons K (1994) Involvement of microtubule motors in basolateral and apical transport in kidney cells. Nature 372:801-803
    • (1994) Nature , vol.372 , pp. 801-803
    • Lafont, F.1    Burkhardt, J.K.2    Simons, K.3
  • 168
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont F, Lecat S, Verkade P, Simons K (1998) Annexin XIIIb associates with lipid microdomains to function in apical delivery. J Cell Biol 142:1413-1427
    • (1998) J Cell Biol , vol.142 , pp. 1413-1427
    • Lafont, F.1    Lecat, S.2    Verkade, P.3    Simons, K.4
  • 169
    • 0033616708 scopus 로고    scopus 로고
    • Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells
    • Lafont F, Verkade P, Galli T, Wimmer C, Louvard D, Simons K (1999) Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells. Proc Natl Acad Sci 96:3734-3738
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 3734-3738
    • Lafont, F.1    Verkade, P.2    Galli, T.3    Wimmer, C.4    Louvard, D.5    Simons, K.6
  • 171
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V a versatile motor for short-range vesicle transport
    • Langford GM (2002) Myosin-V a versatile motor for short-range vesicle transport. Traffic 3:859-865
    • (2002) Traffic , vol.3 , pp. 859-865
    • Langford, G.M.1
  • 173
    • 0031041239 scopus 로고    scopus 로고
    • The neural cell adhesion molecule expresses a tyrosine-independent basolateral sorting signal
    • Le Gall AH, Powell SK, Yeaman CA, Rodriguez-Boulan E (1997) The neural cell adhesion molecule expresses a tyrosine-independent basolateral sorting signal. J Biol Chem 272:4559-4567
    • (1997) J Biol Chem , vol.272 , pp. 4559-4567
    • Le Gall, A.H.1    Powell, S.K.2    Yeaman, C.A.3    Rodriguez-Boulan, E.4
  • 174
    • 0035964402 scopus 로고    scopus 로고
    • Basolateral membrane expression of a K+ channel, Kir 2.3, is directed by a cytoplasmic COOH-terminal domain
    • Le Maout S, Welling PA, Brejon M, Olsen O, Merot J (2001) Basolateral membrane expression of a K+ channel, Kir 2.3, is directed by a cytoplasmic COOH-terminal domain. Proc Natl Acad Sci 98:10475-10480
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 10475-10480
    • Le Maout, S.1    Welling, P.A.2    Brejon, M.3    Olsen, O.4    Merot, J.5
  • 175
    • 0036179747 scopus 로고    scopus 로고
    • A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia
    • Lee S, Fan S, Makarova O, Straight S, Margolis B (2002) A novel and
    • (2002) Mol Cell Biol , vol.22 , pp. 1778-1791
    • Lee, S.1    Fan, S.2    Makarova, O.3    Straight, S.4    Margolis, B.5
  • 176
    • 0014696572 scopus 로고
    • Secretory activity and oncogenicity of a cell line (MDCK) derived from canine kidney
    • Leighton J, Brada Z, Estes LW, Justh G (1969) Secretory activity and oncogenicity of a cell line (MDCK) derived from canine kidney. Science 163:472-473
    • (1969) Science , vol.163 , pp. 472-473
    • Leighton, J.1    Brada, Z.2    Estes, L.W.3    Justh, G.4
  • 177
    • 0034084289 scopus 로고    scopus 로고
    • Sorting of membrane and fluid at the apical pole of polarized Madin-Darby canine kidney cells
    • Leung SM, Ruiz WG, Apodaca G (2000) Sorting of membrane and fluid at the apical pole of polarized Madin-Darby canine kidney cells. Mol Biol Cell 11:2131-2150
    • (2000) Mol Biol Cell , vol.11 , pp. 2131-2150
    • Leung, S.M.1    Ruiz, W.G.2    Apodaca, G.3
  • 178
    • 0036838541 scopus 로고    scopus 로고
    • SNARE expression and localization in renal epithelial cells suggest mechanism for variability of trafficking phenotypes
    • Li X, Low SH, Miura M, Weimbs T (2002) SNARE expression and localization in renal epithelial cells suggest mechanism for variability of trafficking phenotypes. Am J Physiol Renal Physiol 283:F1111-F1122
    • (2002) Am J Physiol Renal Physiol , vol.283
    • Li, X.1    Low, S.H.2    Miura, M.3    Weimbs, T.4
  • 179
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
    • Lin D, Edwards AS, Fawcett JP, Mbamalu G, Scott JD, Pawson T (2000) A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity. Nat Cell Biol 2:540-547
    • (2000) Nat Cell Biol , vol.2 , pp. 540-547
    • Lin, D.1    Edwards, A.S.2    Fawcett, J.P.3    Mbamalu, G.4    Scott, J.D.5    Pawson, T.6
  • 180
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells
    • Lin S, Naim HY, Rodriguez AC, Roth MG (1998) Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells. J Cell Biol 142:51-57
    • (1998) J Cell Biol , vol.142 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, A.C.3    Roth, M.G.4
  • 181
    • 0032498628 scopus 로고    scopus 로고
    • Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells
    • Lipardi C, Mora R, Colomer V, Paladino S, Nitsch L, Rodriguez-Boulan E, Zurzolo C (1998) Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells. J Cell Biol 140:617-626
    • (1998) J Cell Biol , vol.140 , pp. 617-626
    • Lipardi, C.1    Mora, R.2    Colomer, V.3    Paladino, S.4    Nitsch, L.5    Rodriguez-Boulan, E.6    Zurzolo, C.7
  • 182
    • 0034003908 scopus 로고    scopus 로고
    • Detergent-insoluble GPI-anchored proteins are apically sorted in fischer rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting
    • Lipardi C, Nitsch L, Zurzolo C (2000) Detergent-insoluble GPI-anchored proteins are apically sorted in fischer rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting. Mol Biol Cell 11:531-542
    • (2000) Mol Biol Cell , vol.11 , pp. 531-542
    • Lipardi, C.1    Nitsch, L.2    Zurzolo, C.3
  • 183
    • 0033638380 scopus 로고    scopus 로고
    • Exocyst is involved in cystogenesis and tubulogenesis and actsby modulating synthesis and delivery of basolateral plasma membrane and secretory proteins
    • Lipschutz JH, Guo W, O'brien LE, Nguyen YH, Novick P, Mostov KE (2000) Exocyst is involved in cystogenesis and tubulogenesis and actsby modulating synthesis and delivery of basolateral plasma membrane and secretory proteins. Mol Biol Cell 11:4259-4275
    • (2000) Mol Biol Cell , vol.11 , pp. 4259-4275
    • Lipschutz, J.H.1    Guo, W.2    O'brien, L.E.3    Nguyen, Y.H.4    Novick, P.5    Mostov, K.E.6
  • 184
    • 0025133358 scopus 로고
    • Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells
    • Lisanti MP, Caras IW, Gilbert T, Hanzel D, Rodriguez-Boulan E (1990) Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells. Proc Natl Acad Sci 87:7419-7423
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 7419-7423
    • Lisanti, M.P.1    Caras, I.W.2    Gilbert, T.3    Hanzel, D.4    Rodriguez-Boulan, E.5
  • 185
    • 0029847075 scopus 로고    scopus 로고
    • Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells
    • Low SH, Chapin SJ, Weimbs T, Komuves LG, Bennett MK, Mostov KE (1996) Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells. Mol Biol Cell 7:2007-2018
    • (1996) Mol Biol Cell , vol.7 , pp. 2007-2018
    • Low, S.H.1    Chapin, S.J.2    Weimbs, T.3    Komuves, L.G.4    Bennett, M.K.5    Mostov, K.E.6
  • 188
    • 0034490758 scopus 로고    scopus 로고
    • Intracellular redirection of plasma membrane trafficking after loss of epithelial cell polarity
    • Low SH, Miura M, Roche PA, Valdez AC, Mostov KE, Weimbs T (2000) Intracellular redirection of plasma membrane trafficking after loss of epithelial cell polarity. Mol Biol Cell 11:3045-3060
    • (2000) Mol Biol Cell , vol.11 , pp. 3045-3060
    • Low, S.H.1    Miura, M.2    Roche, P.A.3    Valdez, A.C.4    Mostov, K.E.5    Weimbs, T.6
  • 190
    • 0034235509 scopus 로고    scopus 로고
    • Kidney development in cadherin-6 mutants: Delayed mesenchyme-to-epithelial conversion and loss of nephrons
    • Mah SP, Saueressig H, Goulding M, Kintner C, Dressler GR (2000) Kidney development in cadherin-6 mutants: Delayed mesenchyme-to-epithelial conversion and loss of nephrons. Dev Biol 223:38-53
    • (2000) Dev Biol , vol.223 , pp. 38-53
    • Mah, S.P.1    Saueressig, H.2    Goulding, M.3    Kintner, C.4    Dressler, G.R.5
  • 191
    • 0037413672 scopus 로고    scopus 로고
    • Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1)
    • Makarova O, Roh MH, Liu CJ, Laurinec S, Margolis B (2003) Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1) Gene 302:21-29
    • (2003) Gene , vol.302 , pp. 21-29
    • Makarova, O.1    Roh, M.H.2    Liu, C.J.3    Laurinec, S.4    Margolis, B.5
  • 192
    • 0029813157 scopus 로고    scopus 로고
    • Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: Possible role in aquaporin-2 trafficking
    • Mandon B, Chou CL, Nielsen S, Knepper MA (1996) Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: possible role in aquaporin-2 trafficking. J Clin Invest 98:906-913
    • (1996) J Clin Invest , vol.98 , pp. 906-913
    • Mandon, B.1    Chou, C.L.2    Nielsen, S.3    Knepper, M.A.4
  • 194
    • 0030889917 scopus 로고    scopus 로고
    • Both microtubules and actin filaments are required for efficient postendocytotic traffic of the polymeric immunoglobulin receptor in polarized Madin-Darby canine kidney cells
    • Maples CJ, Ruiz WG, Apodaca G (1997) Both microtubules and actin filaments are required for efficient postendocytotic traffic of the polymeric immunoglobulin receptor in polarized Madin-Darby canine kidney cells. J Biol Chem 272:6741-6751
    • (1997) J Biol Chem , vol.272 , pp. 6741-6751
    • Maples, C.J.1    Ruiz, W.G.2    Apodaca, G.3
  • 195
    • 0030041236 scopus 로고    scopus 로고
    • Effect of a dynein inhibitor on vasopressin action in toad urinary bladder
    • Marples D, Barber B, Taylor A (1996) Effect of a dynein inhibitor on vasopressin action in toad urinary bladder. J Physiol 490:767-774
    • (1996) J Physiol , vol.490 , pp. 767-774
    • Marples, D.1    Barber, B.2    Taylor, A.3
  • 196
    • 0031934541 scopus 로고    scopus 로고
    • Dynein and dynactin colocalize with AQP2 water channels in intracellular vesicles from kidney collecting duct
    • Marples D, Schroer TA, Ahrens N, Taylor A, Knepper MA, Nielsen S (1998) Dynein and dynactin colocalize with AQP2 water channels in intracellular vesicles from kidney collecting duct. Am J Physiol 274:F384-F394
    • (1998) Am J Physiol , vol.274
    • Marples, D.1    Schroer, T.A.2    Ahrens, N.3    Taylor, A.4    Knepper, M.A.5    Nielsen, S.6
  • 197
    • 0242668515 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for the overall apical delivery of membrane proteins in the polarized epithelial Madin-Darby canine kidney and fischer rat thyroid cell lines
    • Martin-Belmonte F, Puertollano R, Millan J, Alonso MA (2000) The MAL proteolipid is necessary for the overall apical delivery of membrane proteins in the polarized epithelial Madin-Darby canine kidney and fischer rat thyroid cell lines. Mol Biol Cell 11:2033-2045
    • (2000) Mol Biol Cell , vol.11 , pp. 2033-2045
    • Martin-Belmonte, F.1    Puertollano, R.2    Millan, J.3    Alonso, M.A.4
  • 199
    • 0035859819 scopus 로고    scopus 로고
    • The Sec 6/8 complex in mammalian cells: Characterization of mammalian Sec 3, subunit interactions, and expression of subunits in polarized cells
    • Matern HT, Yeaman C, Nelson WJ, Scheller RH (2001) The Sec 6/8 complex in mammalian cells: Characterization of mammalian Sec 3, subunit interactions, and expression of subunits in polarized cells. Proc Natl Acad Sci 98(17):9648-9653
    • (2001) Proc Natl Acad Sci , vol.98 , Issue.17 , pp. 9648-9653
    • Matern, H.T.1    Yeaman, C.2    Nelson, W.J.3    Scheller, R.H.4
  • 200
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation
    • Matlin KS, Simons K (1983) Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell 34:233-243
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 201
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter K, Mellman I (1994) Mechanisms of cell polarity: Sorting and transport in epithelial cells. Curr Biol 6:545-554
    • (1994) Curr Biol , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 202
    • 0026482992 scopus 로고
    • Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants
    • Matter K, Hunziker W, Mellman I (1992) Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants. Cell 71:741-753
    • (1992) Cell , vol.71 , pp. 741-753
    • Matter, K.1    Hunziker, W.2    Mellman, I.3
  • 203
    • 0027444967 scopus 로고
    • Common signals control low density lipoprotein receptor sorting in endosomes and the Golgi complex of MDCK cells
    • Matter K, Whitney JA, Yamamoto EM, Mellman I (1993) Common signals control low density lipoprotein receptor sorting in endosomes and the Golgi complex of MDCK cells. Cell 74:1053-1064
    • (1993) Cell , vol.74 , pp. 1053-1064
    • Matter, K.1    Whitney, J.A.2    Yamamoto, E.M.3    Mellman, I.4
  • 204
    • 0027989516 scopus 로고
    • Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells
    • Matter K, Yamamoto EM, Mellman I (1994) Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells. J Cell Biol 126:991-1004
    • (1994) J Cell Biol , vol.126 , pp. 991-1004
    • Matter, K.1    Yamamoto, E.M.2    Mellman, I.3
  • 205
    • 0040962408 scopus 로고    scopus 로고
    • Association of neuronal calcium channels with modular adaptor proteins
    • Maximov A, Sudhof TC, Bezprozvanny I (1999) Association of neuronal calcium channels with modular adaptor proteins. J Biol Chem 274:24453-24456
    • (1999) J Biol Chem , vol.274 , pp. 24453-24456
    • Maximov, A.1    Sudhof, T.C.2    Bezprozvanny, I.3
  • 206
    • 0029166488 scopus 로고
    • Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells
    • Mays RW, Siemers KA, Fritz BA, Lowe AW, Van Meer G, Nelson WJ (1995) Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J Cell Biol 130:1105-1115
    • (1995) J Cell Biol , vol.130 , pp. 1105-1115
    • Mays, R.W.1    Siemers, K.A.2    Fritz, B.A.3    Lowe, A.W.4    Van Meer, G.5    Nelson, W.J.6
  • 207
    • 0023139296 scopus 로고
    • Morphogenetic clonal growth of kidney epithelial cell line MDCK
    • Mcateer JA, Evan AP, Gardner KD (1987) Morphogenetic clonal growth of kidney epithelial cell line MDCK. Anat Rec 217:229-239
    • (1987) Anat Rec , vol.217 , pp. 229-239
    • Mcateer, J.A.1    Evan, A.P.2    Gardner, K.D.3
  • 208
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab 5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • Mcbride HM, Rybin V, Murphy C, Giner A, Teasdale R, Zerial M (1999) Oligomeric complexes link Rab 5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 98:377-386
    • (1999) Cell , vol.98 , pp. 377-386
    • Mcbride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 209
    • 0025325815 scopus 로고
    • Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity
    • Mcneill H, Ozawa M, Kemler R, Nelson WJ (1990) Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity. Cell 62:309-316
    • (1990) Cell , vol.62 , pp. 309-316
    • Mcneill, H.1    Ozawa, M.2    Kemler, R.3    Nelson, W.J.4
  • 210
    • 0028832778 scopus 로고
    • Characterization of proteins in detergent-resistant membrane complexes from Madin-Darby canine kidney epithelial cells
    • Melkonian KA, Chu T, Tortorella LB, Brown DA (1995) Characterization of proteins in detergent-resistant membrane complexes from Madin-Darby canine kidney epithelial cells. Biochemistry 34:16161-16170
    • (1995) Biochemistry , vol.34 , pp. 16161-16170
    • Melkonian, K.A.1    Chu, T.2    Tortorella, L.B.3    Brown, D.A.4
  • 211
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I (1996) Endocytosis and molecular sorting. Annu Rev Cell Dev Biol 12:575-625
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 575-625
    • Mellman, I.1
  • 212
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V, Post PL, Mooseker MS (1998) Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 279:527-533
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 213
    • 0031023458 scopus 로고    scopus 로고
    • The MAL proteolipid is a component of the detergent-insoluble membrane subdomains of human T-lymphocytes
    • Millan J, Puertollano R, Fan L, Rancano C, Alonso MA (1997) The MAL proteolipid is a component of the detergent-insoluble membrane subdomains of human T-lymphocytes. Biochem J 321:247-252
    • (1997) Biochem J , vol.321 , pp. 247-252
    • Millan, J.1    Puertollano, R.2    Fan, L.3    Rancano, C.4    Alonso, M.A.5
  • 214
    • 0035933872 scopus 로고    scopus 로고
    • A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • Miranda KC, Khromykh T, Christy P, Le TL, Gottardi CJ, Yap AS, Stow JL, Teasdale RD (2004) A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells. J Biol Chem 276:22565-22572
    • (2004) J Biol Chem , vol.276 , pp. 22565-22572
    • Miranda, K.C.1    Khromykh, T.2    Christy, P.3    Le, T.L.4    Gottardi, C.J.5    Yap, A.S.6    Stow, J.L.7    Teasdale, R.D.8
  • 215
    • 0021677862 scopus 로고
    • Biogenesis of epithelial cell polarity: Intracellular sorting and vectorial exocytosis of an apical plasma membrane glycoprotein
    • Misek DE, Bard E, Rodriguez-Boulan E (1984) Biogenesis of epithelial cell polarity: Intracellular sorting and vectorial exocytosis of an apical plasma membrane glycoprotein. Cell 39:537-546
    • (1984) Cell , vol.39 , pp. 537-546
    • Misek, D.E.1    Bard, E.2    Rodriguez-Boulan, E.3
  • 216
    • 0033520479 scopus 로고    scopus 로고
    • Caveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1
    • Mora R, Bonilha VL, Marmorstein A, Scherer PE, Brown D, Lisanti MP, Rodriguez-Boulan E (1999) Caveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1. J Biol Chem 274:25708-25717
    • (1999) J Biol Chem , vol.274 , pp. 25708-25717
    • Mora, R.1    Bonilha, V.L.2    Marmorstein, A.3    Scherer, P.E.4    Brown, D.5    Lisanti, M.P.6    Rodriguez-Boulan, E.7
  • 217
    • 0036242467 scopus 로고    scopus 로고
    • Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton
    • Morris SM, Arden SD, Roberts RC, Kendrick-Jones J, Cooper JA, Luzio JP, Buss F (2004) Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton. Traffic 3:331-341
    • (2004) Traffic , vol.3 , pp. 331-341
    • Morris, S.M.1    Arden, S.D.2    Roberts, R.C.3    Kendrick-Jones, J.4    Cooper, J.A.5    Luzio, J.P.6    Buss, F.7
  • 218
    • 0024571516 scopus 로고
    • Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells
    • Morrow JS, Cianci CD, Ardito T, Mann AS, Kashgarian M (1989) Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. J Cell Biol 108:455-465
    • (1989) J Cell Biol , vol.108 , pp. 455-465
    • Morrow, J.S.1    Cianci, C.D.2    Ardito, T.3    Mann, A.S.4    Kashgarian, M.5
  • 220
    • 0346154744 scopus 로고    scopus 로고
    • Ral GTPases regulate exocyst assembly through dual subunit interactions
    • (in press)
    • Moskalenko S, Tong C, Rosse C, Camonis J, White MA (2003) Ral GTPases regulate exocyst assembly through dual subunit interactions. J Biol Chem (in press)
    • (2003) J Biol Chem
    • Moskalenko, S.1    Tong, C.2    Rosse, C.3    Camonis, J.4    White, M.A.5
  • 224
    • 0029903396 scopus 로고    scopus 로고
    • Amadillo, bazooka, and stardust are critical for early stages in formation of the zonula adherens and maintenance of the polarized blastoderm epithelium in Drosophila
    • Muller HA, Wieschaus E (1996) Amadillo, bazooka, and stardust are critical for early stages in formation of the zonula adherens and maintenance of the polarized blastoderm epithelium in Drosophila. J Cell Biol 134:149-163
    • (1996) J Cell Biol , vol.134 , pp. 149-163
    • Muller, H.A.1    Wieschaus, E.2
  • 225
    • 0040971539 scopus 로고    scopus 로고
    • Myosin II is involved in the production of constitutive transport vesicles from the TGN
    • Musch A, Cohen D, Rodriguez-Boulan E (1997) Myosin II is involved in the production of constitutive transport vesicles from the TGN J Cell Biol 138:291-301
    • (1997) J Cell Biol , vol.138 , pp. 291-301
    • Musch, A.1    Cohen, D.2    Rodriguez-Boulan, E.3
  • 226
    • 0035341316 scopus 로고    scopus 로고
    • cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network
    • Musch A, Cohen D, Kreitzer G, Rodriguez-Boulan E (2001) cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J 20:2171-2179
    • (2001) EMBO J , vol.20 , pp. 2171-2179
    • Musch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 227
    • 0036156362 scopus 로고    scopus 로고
    • Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells
    • Musch A, Cohen D, Yeaman C, Nelson WJ, Rodriguez-Boulan E, Brennwald PJ (2002) Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells. Mol Biol Cell 13:158-168
    • (2002) Mol Biol Cell , vol.13 , pp. 158-168
    • Musch, A.1    Cohen, D.2    Yeaman, C.3    Nelson, W.J.4    Rodriguez-Boulan, E.5    Brennwald, P.J.6
  • 228
    • 0032475976 scopus 로고    scopus 로고
    • Identification of sorting determinants in the C-terminal cytoplasmic tails of the gamma-aminobutyric acid transporters GAT-2 and GAT-3
    • Muth TR, Ahn J, Caplan MJ (1998) Identification of sorting determinants in the C-terminal cytoplasmic tails of the gamma-aminobutyric acid transporters GAT-2 and GAT-3. J Biol Chem 273:25616-25627
    • (1998) J Biol Chem , vol.273 , pp. 25616-25627
    • Muth, T.R.1    Ahn, J.2    Caplan, M.J.3
  • 229
    • 0344875494 scopus 로고    scopus 로고
    • The adaptor protein ARH escorts megalin to and through endosomes
    • Nagai M, Meerloo T, Takeda T, Farquhar MG (2003) The adaptor protein ARH escorts megalin to and through endosomes. Mol Biol Cell 14:4984-4996
    • (2003) Mol Biol Cell , vol.14 , pp. 4984-4996
    • Nagai, M.1    Meerloo, T.2    Takeda, T.3    Farquhar, M.G.4
  • 230
    • 0036828968 scopus 로고    scopus 로고
    • Regulated protein-protein interaction between aPKC and PAR-3 plays an essential role in the polarization of epithelial cells
    • Nagai-Tamai Y, Mizuno K, Hirose T, Suzuki A, Ohno S (2002) Regulated protein-protein interaction between aPKC and PAR-3 plays an essential role in the polarization of epithelial cells. Genes Cells 7:1161-1171
    • (2002) Genes Cells , vol.7 , pp. 1161-1171
    • Nagai-Tamai, Y.1    Mizuno, K.2    Hirose, T.3    Suzuki, A.4    Ohno, S.5
  • 231
    • 0033776810 scopus 로고    scopus 로고
    • Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase
    • Nakagawa S, Huibregtse JM (2000) Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase. Mol Cell Biol 20:8244-8253
    • (2000) Mol Cell Biol , vol.20 , pp. 8244-8253
    • Nakagawa, S.1    Huibregtse, J.M.2
  • 232
    • 0028289669 scopus 로고
    • Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells
    • Nathke IS, Hinck L, Swedlow JR, Papkoff J, Nelson WJ (1994) Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells. J Cell Biol 125:1341-1352
    • (1994) J Cell Biol , vol.125 , pp. 1341-1352
    • Nathke, I.S.1    Hinck, L.2    Swedlow, J.R.3    Papkoff, J.4    Nelson, W.J.5
  • 233
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, beta-catenin, and cadherin pathways
    • Nelson WJ, Nusse R (2004) Convergence of Wnt, beta-catenin, and cadherin pathways. Science 303:1483-1487
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 234
    • 0023262074 scopus 로고
    • Ankyrin binding to (Na+ + K+)ATPase and implications for the organization of membrane domains in polarized cells
    • Nelson WJ, Veshnock PJ (1987) Ankyrin binding to (Na+ + K+)ATPase and implications for the organization of membrane domains in polarized cells. Nature 328:533-536
    • (1987) Nature , vol.328 , pp. 533-536
    • Nelson, W.J.1    Veshnock, P.J.2
  • 235
    • 0025125799 scopus 로고
    • Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells
    • Nelson WJ, Shore EM, Wang AZ, Hammerton RW (1990) Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells. J Cell Biol 110:349-357
    • (1990) J Cell Biol , vol.110 , pp. 349-357
    • Nelson, W.J.1    Shore, E.M.2    Wang, A.Z.3    Hammerton, R.W.4
  • 236
    • 0028972114 scopus 로고
    • Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles. Colocalization with Aquaporin-2 water channels
    • Nielsen S, Marples D, Birn H, Mohtashami M, Dalby NO, Trimble M, Knepper M (1995) Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles. Colocalization with Aquaporin-2 water channels. J Clin Invest 96:1834-1844
    • (1995) J Clin Invest , vol.96 , pp. 1834-1844
    • Nielsen, S.1    Marples, D.2    Birn, H.3    Mohtashami, M.4    Dalby, N.O.5    Trimble, M.6    Knepper, M.7
  • 237
    • 0035494465 scopus 로고    scopus 로고
    • KIFC3 a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranes
    • Noda Y, Okada Y, Saito N, Setou M, Xu Y, Zhang Z, Hirokawa N (2001) KIFC3 a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranes. J Cell Biol 155:77-88
    • (2001) J Cell Biol , vol.155 , pp. 77-88
    • Noda, Y.1    Okada, Y.2    Saito, N.3    Setou, M.4    Xu, Y.5    Zhang, Z.6    Hirokawa, N.7
  • 240
    • 0030905888 scopus 로고    scopus 로고
    • Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells
    • Odorizzi G, Trowbridge IS (1997) Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells. J Cell Biol 137:1255-1264
    • (1997) J Cell Biol , vol.137 , pp. 1255-1264
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 241
    • 0029820888 scopus 로고    scopus 로고
    • Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism
    • Odorizzi G, Pearse A, Domingo D, Trowbridge IS, Hopkins CR (1996) Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism. J Cell Biol 135:139-152
    • (1996) J Cell Biol , vol.135 , pp. 139-152
    • Odorizzi, G.1    Pearse, A.2    Domingo, D.3    Trowbridge, I.S.4    Hopkins, C.R.5
  • 243
    • 0029826535 scopus 로고    scopus 로고
    • Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains
    • Ohno H, Fournier MC, Poy G, Bonifacino JS (1996) Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains. J Biol Chem 271:29009-29015
    • (1996) J Biol Chem , vol.271 , pp. 29009-29015
    • Ohno, H.1    Fournier, M.C.2    Poy, G.3    Bonifacino, J.S.4
  • 244
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno H, Aguilar RC, Yeh D, Taura D, Saito T, Bonifacino JS (1998) The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J Biol Chem 273:25915-25921
    • (1998) J Biol Chem , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saito, T.5    Bonifacino, J.S.6
  • 246
    • 0024202621 scopus 로고
    • The polarized distribution of an apical cell surface glycoprotein is maintained by interactions with the cytoskeleton of Madin-Darby canine kidney cells
    • Ojakian GK, Schwimmer R (1988) The polarized distribution of an apical cell surface glycoprotein is maintained by interactions with the cytoskeleton of Madin-Darby canine kidney cells. J Cell Biol 107:2377-2387
    • (1988) J Cell Biol , vol.107 , pp. 2377-2387
    • Ojakian, G.K.1    Schwimmer, R.2
  • 247
    • 0031465172 scopus 로고    scopus 로고
    • Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
    • Okamoto M, Sudhof TC (1997) Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. J Biol Chem 272:31459-31464
    • (1997) J Biol Chem , vol.272 , pp. 31459-31464
    • Okamoto, M.1    Sudhof, T.C.2
  • 248
    • 0036076755 scopus 로고    scopus 로고
    • Basolateral membrane expression of the Kir 2.3 channel is coordinated by PDZ interaction with Lin-7/CASK complex
    • Olsen O, Liu H, Wade JB, Merot J, Welling PA (2002) Basolateral membrane expression of the Kir 2.3 channel is coordinated by PDZ interaction with Lin-7/CASK complex. Am J Physiol Cell Physiol 282:C183-C195
    • (2002) Am J Physiol Cell Physiol , vol.282
    • Olsen, O.1    Liu, H.2    Wade, J.B.3    Merot, J.4    Welling, P.A.5
  • 249
    • 0034685896 scopus 로고    scopus 로고
    • Interactions between the exocytic and endocytic pathways in polarized Madin-Darby canine kidney cells
    • Orzech E, Cohen S, Weiss A, Aroeti B (2000) Interactions between the exocytic and endocytic pathways in polarized Madin-Darby canine kidney cells. J Biol Chem 275:15207-15219
    • (2000) J Biol Chem , vol.275 , pp. 15207-15219
    • Orzech, E.1    Cohen, S.2    Weiss, A.3    Aroeti, B.4
  • 250
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen DJ, Evans PR (1998) A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282:1327-1332
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 251
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade G (1975) Intracellular aspects of the process of protein synthesis. Science 189:347-358
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 252
    • 0024810856 scopus 로고
    • Meeting of the apical and basolateral endocytic pathways of the Madin-Darby canine kidney cell in late endosomes
    • Parton RG, Prydz K, Bomsel M, Simons K, Griffiths G (1989) Meeting of the apical and basolateral endocytic pathways of the Madin-Darby canine kidney cell in late endosomes. J Cell Biol 109:3259-3272
    • (1989) J Cell Biol , vol.109 , pp. 3259-3272
    • Parton, R.G.1    Prydz, K.2    Bomsel, M.3    Simons, K.4    Griffiths, G.5
  • 253
    • 0035279058 scopus 로고    scopus 로고
    • SNAREs and the specificity of membrane fusion
    • Pelham HR (2001) SNAREs and the specificity of membrane fusion. Trends Cell Biol 11:99-101
    • (2001) Trends Cell Biol , vol.11 , pp. 99-101
    • Pelham, H.R.1
  • 254
    • 0030941972 scopus 로고    scopus 로고
    • Sorting of two polytopic proteins, the gamma-aminobutyric acid and betaine transporters, in polarized epithelial cells
    • Perego C, Bulbarelli A, Longhi R, Caimi M, Villa A, Caplan MJ (1997) Sorting of two polytopic proteins, the gamma-aminobutyric acid and betaine transporters, in polarized epithelial cells. J Biol Chem 272:6584-6592
    • (1997) J Biol Chem , vol.272 , pp. 6584-6592
    • Perego, C.1    Bulbarelli, A.2    Longhi, R.3    Caimi, M.4    Villa, A.5    Caplan, M.J.6
  • 255
    • 0033522488 scopus 로고    scopus 로고
    • PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells
    • Perego C, Vanoni C, Villa A, Longhi R, Kaech SM, Frohli E, Hajnal A, Kim SK, Pietrini G (1999) PDZ-mediated interactions retain the epithelial GABA transporter on the basolateral surface of polarized epithelial cells. EMBO J 18:2384-2393
    • (1999) EMBO J , vol.18 , pp. 2384-2393
    • Perego, C.1    Vanoni, C.2    Villa, A.3    Longhi, R.4    Kaech, S.M.5    Frohli, E.6    Hajnal, A.7    Kim, S.K.8    Pietrini, G.9
  • 256
    • 0022390726 scopus 로고
    • Intracellular sorting and basolateral appearance of the G protein of vesicular stomatitis virus in Madin-Darby canine kidney cells
    • Pfeiffer S, Fuller SD, Simons K (1985) Intracellular sorting and basolateral appearance of the G protein of vesicular stomatitis virus in Madin-Darby canine kidney cells. J Cell Biol 101:470-476
    • (1985) J Cell Biol , vol.101 , pp. 470-476
    • Pfeiffer, S.1    Fuller, S.D.2    Simons, K.3
  • 257
    • 2342599664 scopus 로고    scopus 로고
    • Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway
    • Polishchuk R, Pentima AD, Lippincott-Schwartz J (2004) Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway. Nat Cell Biol 6:297-307
    • (2004) Nat Cell Biol , vol.6 , pp. 297-307
    • Polishchuk, R.1    Pentima, A.D.2    Lippincott-Schwartz, J.3
  • 258
    • 1542313963 scopus 로고    scopus 로고
    • Specific N-glycans direct apical delivery of transmembrane, but not soluble or glycosylphosphatidylinositol-anchored forms of endolyn in Madin-Darby canine kidney cells
    • Potter BA, Ihrke G, Bruns JR, Weixel KM, Weisz OA (2004) Specific N-glycans direct apical delivery of transmembrane, but not soluble or glycosylphosphatidylinositol-anchored forms of endolyn in Madin-Darby canine kidney cells. Mol Biol Cell 15:1407-1416
    • (2004) Mol Biol Cell , vol.15 , pp. 1407-1416
    • Potter, B.A.1    Ihrke, G.2    Bruns, J.R.3    Weixel, K.M.4    Weisz, O.A.5
  • 259
    • 0025874210 scopus 로고
    • Targeting of transmembrane and GPI-anchored forms of N-CAM to opposite domains of a polarized epithelial cell
    • Powell SK, Cunningham BA, Edelman GM, Rodriguez-Boulan E (1991) Targeting of transmembrane and GPI-anchored forms of N-CAM to opposite domains of a polarized epithelial cell. Nature 353:76-77
    • (1991) Nature , vol.353 , pp. 76-77
    • Powell, S.K.1    Cunningham, B.A.2    Edelman, G.M.3    Rodriguez-Boulan, E.4
  • 260
    • 0034502463 scopus 로고    scopus 로고
    • A Rab 11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes
    • Prekeris R, Klumperman J, Scheller RH (2000) A Rab 11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes. Mol Cell 6:1437-1438
    • (2000) Mol Cell , vol.6 , pp. 1437-1438
    • Prekeris, R.1    Klumperman, J.2    Scheller, R.H.3
  • 261
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells
    • Puertollano R, Martin-Belmonte F, Millan J, De Marco MC, Albar JP, Kremer L, Alonso MA (1999) The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells. J Cell Biol 145:141-151
    • (1999) J Cell Biol , vol.145 , pp. 141-151
    • Puertollano, R.1    Martin-Belmonte, F.2    Millan, J.3    De Marco, M.C.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 263
    • 0345237979 scopus 로고    scopus 로고
    • Syntaxin 2 splice variants exhibit differential expression patterns, biochemical properties and subcellular localizations
    • Quinones B, Riento K, Olkkonen VM, Hardy S, Bennett MK (1999) Syntaxin 2 splice variants exhibit differential expression patterns, biochemical properties and subcellular localizations. J Cell Sci 112:4291-4304
    • (1999) J Cell Sci , vol.112 , pp. 4291-4304
    • Quinones, B.1    Riento, K.2    Olkkonen, V.M.3    Hardy, S.4    Bennett, M.K.5
  • 264
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions
    • Rajasekaran AK, Hojo M, Huima T, Rodriguez-Boulan E (1996) Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions. J Cell Biol 132:451-463
    • (1996) J Cell Biol , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 265
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapoport I, Chen YC, Cupers P, Shoelson SE, Kirchhausen T (1998) Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J 17:2148-2155
    • (1998) EMBO J , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 266
    • 0029831485 scopus 로고    scopus 로고
    • The basolateral sorting signal of the polymeric immunoglobulin receptor contains two functional domains
    • Reich V, Mostov K, Aroeti B (1996) The basolateral sorting signal of the polymeric immunoglobulin receptor contains two functional domains. J Cell Sci 109:2133-2139
    • (1996) J Cell Sci , vol.109 , pp. 2133-2139
    • Reich, V.1    Mostov, K.2    Aroeti, B.3
  • 267
    • 0031966321 scopus 로고    scopus 로고
    • E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton
    • Reuver SM, Garner CC (1998) E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton. J Cell Sci 111:1071-1080
    • (1998) J Cell Sci , vol.111 , pp. 1071-1080
    • Reuver, S.M.1    Garner, C.C.2
  • 268
    • 0031669173 scopus 로고    scopus 로고
    • Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells
    • Riento K, Galli T, Jansson S, Ehnholm C, Lehtonen E, Olkkonen VM (1998) Interaction of Munc-18-2 with syntaxin 3 controls the association of apical SNAREs in epithelial cells. J Cell Sci 111:2681-2688
    • (1998) J Cell Sci , vol.111 , pp. 2681-2688
    • Riento, K.1    Galli, T.2    Jansson, S.3    Ehnholm, C.4    Lehtonen, E.5    Olkkonen, V.M.6
  • 269
    • 0021186349 scopus 로고
    • Viral glycoproteins destined for apical or basolateral plasma membrane domains traverse the same Golgi apparatus during their intracellular transport in doubly infected Madin-Darby canine kidney cells
    • Rindler MJ, Ivanov IE, Plesken H, Rodriguez-Boulan E, Sabatini DD (1984) Viral glycoproteins destined for apical or basolateral plasma membrane domains traverse the same Golgi apparatus during their intracellular transport in doubly infected Madin-Darby canine kidney cells. J Cell Biol 98:1304-1319
    • (1984) J Cell Biol , vol.98 , pp. 1304-1319
    • Rindler, M.J.1    Ivanov, I.E.2    Plesken, H.3    Rodriguez-Boulan, E.4    Sabatini, D.D.5
  • 270
    • 0023293841 scopus 로고
    • Microtubule-acting drugs lead to the nonpolarized delivery of the influenza hemagglutinin to the cell surface of polarized Madin-Darby canine kidney cells
    • Rindler MJ, Ivanov IE, Sabatini DD (1987) Microtubule-acting drugs lead to the nonpolarized delivery of the influenza hemagglutinin to the cell surface of polarized Madin-Darby canine kidney cells. J Cell Biol 104:231-241
    • (1987) J Cell Biol , vol.104 , pp. 231-241
    • Rindler, M.J.1    Ivanov, I.E.2    Sabatini, D.D.3
  • 272
    • 0036500526 scopus 로고    scopus 로고
    • Human myosin-Vc is a novel class V myosin expressed in epithelial cells
    • Rodriguez OC, Cheney RE (2002) Human myosin-Vc is a novel class V myosin expressed in epithelial cells. J Cell Sci 115:991-1004
    • (2002) J Cell Sci , vol.115 , pp. 991-1004
    • Rodriguez, O.C.1    Cheney, R.E.2
  • 273
    • 0033179221 scopus 로고    scopus 로고
    • Glycans in post-Golgi apical targeting: Sorting signals or structural props?
    • Rodriguez-Boulan E, Gonzalez A (1999) Glycans in post-Golgi apical targeting: Sorting signals or structural props? Trends Cell Biol 9:291-224
    • (1999) Trends Cell Biol , vol.9 , pp. 224-291
    • Rodriguez-Boulan, E.1    Gonzalez, A.2
  • 274
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • Rodriguez-Boulan E, Nelson WJ (1989) Morphogenesis of the polarized epithelial cell phenotype. Science 245:718-725
    • (1989) Science , vol.245 , pp. 718-725
    • Rodriguez-Boulan, E.1    Nelson, W.J.2
  • 275
    • 0018853480 scopus 로고
    • Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells
    • Rodriguez-Boulan ER, Pendergast M (1980) Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells. Cell 20:45-54
    • (1980) Cell , vol.20 , pp. 45-54
    • Rodriguez-Boulan, E.R.1    Pendergast, M.2
  • 276
    • 0000747079 scopus 로고
    • Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity
    • Rodriguez-Boulan ER, Sabatini DD (1978) Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity. Proc Natl Acad Sci 75:5071-5075
    • (1978) Proc Natl Acad Sci , vol.75 , pp. 5071-5075
    • Rodriguez-Boulan, E.R.1    Sabatini, D.D.2
  • 277
    • 0020569368 scopus 로고
    • Assembly of enveloped viruses in Madin-Darby canine kidney cells: Polarized budding from single attached cells and from clusters of cells in suspension
    • Rodriguez-Boulan E, Paskiet KT, Sabatini DD (1983) Assembly of enveloped viruses in Madin-Darby canine kidney cells: Polarized budding from single attached cells and from clusters of cells in suspension. J Cell Biol 96:866-874
    • (1983) J Cell Biol , vol.96 , pp. 866-874
    • Rodriguez-Boulan, E.1    Paskiet, K.T.2    Sabatini, D.D.3
  • 278
    • 0021350457 scopus 로고
    • Intracellular transport of influenza virus hemagglutinin to the apical surface of Madin-Darby canine kidney cells
    • Rodriguez-Boulan E, Paskiet KT, Salas PJ, Bard E (1984) Intracellular transport of influenza virus hemagglutinin to the apical surface of Madin-Darby canine kidney cells. J Cell Biol 98:308-319
    • (1984) J Cell Biol , vol.98 , pp. 308-319
    • Rodriguez-Boulan, E.1    Paskiet, K.T.2    Salas, P.J.3    Bard, E.4
  • 279
    • 0037178864 scopus 로고    scopus 로고
    • The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions
    • Roh MH, Liu CJ, Laurinec S, Margolis B (2002a) The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions. J Biol Chem 277:27501-27509
    • (2002) J Biol Chem , vol.277 , pp. 27501-27509
    • Roh, M.H.1    Liu, C.J.2    Laurinec, S.3    Margolis, B.4
  • 281
    • 0036902323 scopus 로고    scopus 로고
    • Immunoglobulin transport across polarized epithelial cells
    • Rojas R, Apodaca G (2002) Immunoglobulin transport across polarized epithelial cells. Nat Rev Mol Cell Biol 3:944-955
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 944-955
    • Rojas, R.1    Apodaca, G.2
  • 282
    • 0034282003 scopus 로고    scopus 로고
    • Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane
    • Roper K, Corbeil D, Huttner WB (2000) Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane. Nat Cell Biol 2:582-592
    • (2000) Nat Cell Biol , vol.2 , pp. 582-592
    • Roper, K.1    Corbeil, D.2    Huttner, W.B.3
  • 283
    • 0030023904 scopus 로고    scopus 로고
    • VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues
    • Rossetto O, Gorza L, Schiavo G, Schiavo N, Scheller RH, Montecucco C (1996) VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues. J Cell Biol 132:167-179
    • (1996) J Cell Biol , vol.132 , pp. 167-179
    • Rossetto, O.1    Gorza, L.2    Schiavo, G.3    Schiavo, N.4    Scheller, R.H.5    Montecucco, C.6
  • 284
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE (1994) Mechanisms of intracellular protein transport. Nature 372:55-63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 285
    • 0032500602 scopus 로고    scopus 로고
    • Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • Roush DL, Gottardi CJ, Naim HY, Roth MG, Caplan MJ (1998) Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells. J Biol Chem 273:26862-26869
    • (1998) J Biol Chem , vol.273 , pp. 26862-26869
    • Roush, D.L.1    Gottardi, C.J.2    Naim, H.Y.3    Roth, M.G.4    Caplan, M.J.5
  • 286
    • 0034773037 scopus 로고    scopus 로고
    • Syntaxin 1A is delivered to the apical and basolateral domains of epithelial cells: The role of munc-18 proteins
    • Rowe J, Calegari F, Taverna E, Longhi R, Rosa P (2001) Syntaxin 1A is delivered to the apical and basolateral domains of epithelial cells: The role of munc-18 proteins. J Cell Sci 114:3323-3332
    • (2001) J Cell Sci , vol.114 , pp. 3323-3332
    • Rowe, J.1    Calegari, F.2    Taverna, E.3    Longhi, R.4    Rosa, P.5
  • 287
    • 0028921036 scopus 로고
    • The AQP2 water channel: Effect of vasopressin treatment, microtubule disruption, and distribution in neonatal rats
    • Sabolic I, Katsura T, Verbavatz JM, Brown D (1995) The AQP2 water channel: Effect of vasopressin treatment, microtubule disruption, and distribution in neonatal rats. J Mol Biol 143:165-175
    • (1995) J Mol Biol , vol.143 , pp. 165-175
    • Sabolic, I.1    Katsura, T.2    Verbavatz, J.M.3    Brown, D.4
  • 288
    • 0036231332 scopus 로고    scopus 로고
    • NHE3 and NHERF are targeted to the basolateral membrane in proximal tubules of colchicine-treated rats
    • Sabolic I, Herak-Kramberger CM, Ljubojevic M, Biemesderfer D, Brown D (2002) NHE3 and NHERF are targeted to the basolateral membrane in proximal tubules of colchicine-treated rats. Kidney Int 61:1351-1364
    • (2002) Kidney Int , vol.61 , pp. 1351-1364
    • Sabolic, I.1    Herak-Kramberger, C.M.2    Ljubojevic, M.3    Biemesderfer, D.4    Brown, D.5
  • 289
    • 0028834898 scopus 로고
    • Loss of MDCK cell alpha 2 beta 1 integrin expression results in reduced cyst formation, failure of hepatocyte growth factor/scatter factor-induced branching morphogenesis, and increased apoptosis
    • Saelman EU, Keely PJ, Santoro SA (1995) Loss of MDCK cell alpha 2 beta 1 integrin expression results in reduced cyst formation, failure of hepatocyte growth factor/scatter factor-induced branching morphogenesis, and increased apoptosis. J Cell Sci 108:3531-3540
    • (1995) J Cell Sci , vol.108 , pp. 3531-3540
    • Saelman, E.U.1    Keely, P.J.2    Santoro, S.A.3
  • 290
    • 0024253418 scopus 로고
    • Selective anchoring in the specific plasma membrane domain: A role in epithelial cell polarity
    • Salas PJ, Vega-Salas DE, Hochman J, Rodriguez-Boulan E, Edidin M (1988) Selective anchoring in the specific plasma membrane domain: A role in epithelial cell polarity. J Cell Biol 107:2363-2376
    • (1988) J Cell Biol , vol.107 , pp. 2363-2376
    • Salas, P.J.1    Vega-Salas, D.E.2    Hochman, J.3    Rodriguez-Boulan, E.4    Edidin, M.5
  • 293
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste J, Kuismanen E (1984) Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38:535-549
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 294
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z, Lisanti MP (1993) Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 122:789-807
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 295
    • 0030877171 scopus 로고    scopus 로고
    • Disruption of microtubules reveals two independent apical targeting mechanisms for G-protein-coupled receptors in polarized renal epithelial cells
    • Saunders C, Limbird LE (1997) Disruption of microtubules reveals two independent apical targeting mechanisms for G-protein-coupled receptors in polarized renal epithelial cells. J Biol Chem 272:19035-19045
    • (1997) J Biol Chem , vol.272 , pp. 19035-19045
    • Saunders, C.1    Limbird, L.E.2
  • 296
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele P, Peranen J, Simons K (1995) N-glycans as apical sorting signals in epithelial cells. Nature 378:96-98
    • (1995) Nature , vol.378 , pp. 96-98
    • Scheiffele, P.1    Peranen, J.2    Simons, K.3
  • 297
    • 0032575477 scopus 로고    scopus 로고
    • Rab GTPases, directors of vesicle docking
    • Schimmoller F, Simon I, Pfeffer SR (1998) Rab GTPases, directors of vesicle docking. J Biol Chem 273:22161-22164
    • (1998) J Biol Chem , vol.273 , pp. 22161-22164
    • Schimmoller, F.1    Simon, I.2    Pfeffer, S.R.3
  • 298
    • 0036144372 scopus 로고    scopus 로고
    • Acid incubation reverses the polarity of intercalated cell transporters, an effect mediated by hensin
    • Schwartz GJ, Tsuruoka S, Vijayakumar S, Petrovic S, Mian A, Al-Awqati Q (2002) Acid incubation reverses the polarity of intercalated cell transporters, an effect mediated by hensin. J Clin Invest 109:89-99
    • (2002) J Clin Invest , vol.109 , pp. 89-99
    • Schwartz, G.J.1    Tsuruoka, S.2    Vijayakumar, S.3    Petrovic, S.4    Mian, A.5    Al-Awqati, Q.6
  • 299
    • 0028978235 scopus 로고
    • The alpha 2 beta 1 integrin regulates collagen-mediated MDCK epithelial membrane remodeling and tubule formation
    • Schwimmer R, Ojakian GK (1995) The alpha 2 beta 1 integrin regulates collagen-mediated MDCK epithelial membrane remodeling and tubule formation. J Cell Sci 108:2487-2498
    • (1995) J Cell Sci , vol.108 , pp. 2487-2498
    • Schwimmer, R.1    Ojakian, G.K.2
  • 300
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • Scott DB, Blanpied TA, Swanson GT, Zhang C, Ehlers MD (2001) An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing. J Neurosci 21:3063-3072
    • (2001) J Neurosci , vol.21 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 301
    • 0037151048 scopus 로고    scopus 로고
    • A novel PDZ protein regulates the activity of guanylyl cyclase C, the heat-stable enterotoxin receptor
    • Scott RO, Thelin WR, Milgram SL (2002) A novel PDZ protein regulates the activity of guanylyl cyclase C, the heat-stable enterotoxin receptor. J Biol Chem 277:22934-22941
    • (2002) J Biol Chem , vol.277 , pp. 22934-22941
    • Scott, R.O.1    Thelin, W.R.2    Milgram, S.L.3
  • 302
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport
    • Setou M, Nakagawa T, Seog DH, Hirokawa N (2000) Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science 288:1796-1802
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 303
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff DR, Daro EA, Hull M, Mellman I (1999) The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J Cell Biol 145:123-139
    • (1999) J Cell Biol , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 304
    • 0036156444 scopus 로고    scopus 로고
    • Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes
    • Sheff DR, Kroschewski R, Mellman I (2002) Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes. Mol Biol Cell 13:262-275
    • (2002) Mol Biol Cell , vol.13 , pp. 262-275
    • Sheff, D.R.1    Kroschewski, R.2    Mellman, I.3
  • 305
    • 17544383706 scopus 로고    scopus 로고
    • A di-hydrophobic Leu-Val motif regulates the basolateral localization of CD44 in polarized Madin-Darby canine kidney epithelial cells
    • Sheikh H, Isacke CM (1996) A di-hydrophobic Leu-Val motif regulates the basolateral localization of CD44 in polarized Madin-Darby canine kidney epithelial cells. J Biol Chem 271:12185-12190
    • (1996) J Biol Chem , vol.271 , pp. 12185-12190
    • Sheikh, H.1    Isacke, C.M.2
  • 306
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M, Sala C (2001) PDZ domains and the organization of supramolecular complexes. Annu Rev Neurosci 24:1-29
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 308
    • 0037143761 scopus 로고    scopus 로고
    • Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting
    • Shenolikar S, Voltz JW, Minkoff CM, Wade JB, Weinman EJ (2002) Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting. Proc Natl Acad Sci 99:11470-11475
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 11470-11475
    • Shenolikar, S.1    Voltz, J.W.2    Minkoff, C.M.3    Wade, J.B.4    Weinman, E.J.5
  • 310
    • 0031921773 scopus 로고    scopus 로고
    • Fluid-phase markers in the basolateral endocytic pathway accumulate in response to the actin assembly-promoting drug Jasplakinolide
    • Shurety W, Stewart NL, Stow JL (1998) Fluid-phase markers in the basolateral endocytic pathway accumulate in response to the actin assembly-promoting drug Jasplakinolide. Mol Biol Cell 9:957-975
    • (1998) Mol Biol Cell , vol.9 , pp. 957-975
    • Shurety, W.1    Stewart, N.L.2    Stow, J.L.3
  • 311
    • 0032913573 scopus 로고    scopus 로고
    • Basolateral sorting of furin in MDCK cells requires a phenylalanine-isoleucine motif together with an acidic amino acid cluster
    • Simmen T, Nobile M, Bonifacino JS, Hunziker W (1999) Basolateral sorting of furin in MDCK cells requires a phenylalanine-isoleucine motif together with an acidic amino acid cluster. Mol Cell Biol 19:3136-3144
    • (1999) Mol Cell Biol , vol.19 , pp. 3136-3144
    • Simmen, T.1    Nobile, M.2    Bonifacino, J.S.3    Hunziker, W.4
  • 312
    • 0036167130 scopus 로고    scopus 로고
    • AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells
    • Simmen T, Honing S, Icking A, Tikkanen R, Hunziker W (2002) AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells. Nat Cell Biol 4:154-159
    • (2002) Nat Cell Biol , vol.4 , pp. 154-159
    • Simmen, T.1    Honing, S.2    Icking, A.3    Tikkanen, R.4    Hunziker, W.5
  • 313
    • 0032477853 scopus 로고    scopus 로고
    • Coatomer, but not P200/myosin II, is required for the in vitro formation of trans-Golgi network-derived vesicles containing the envelope glycoprotein of vesicular stomatitis virus
    • Simon JP, Shen TH, Ivanov IE, Gravotta D, Morimoto T, Adesnik M, Sabatini DD (1998) Coatomer, but not P200/myosin II, is required for the in vitro formation of trans-Golgi network-derived vesicles containing the envelope glycoprotein of vesicular stomatitis virus. Proc Natl Acad Sci 95:1073-1080
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 1073-1080
    • Simon, J.P.1    Shen, T.H.2    Ivanov, I.E.3    Gravotta, D.4    Morimoto, T.5    Adesnik, M.6    Sabatini, D.D.7
  • 314
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K, Van Meer G (1988) Lipid sorting in epithelial cells. Biochemistry 27:6197-6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 316
    • 0032879685 scopus 로고    scopus 로고
    • The Rab 5 effector EEA1 interacts directly with syntaxin-6
    • Simonsen A, Gaullier JM, D'arrigo A, Stenmark H (1999a) The Rab 5 effector EEA1 interacts directly with syntaxin-6. J Biol Chem 274:28857-28860
    • (1999) J Biol Chem , vol.274 , pp. 28857-28860
    • Simonsen, A.1    Gaullier, J.M.2    D'arrigo, A.3    Stenmark, H.4
  • 317
    • 0033197976 scopus 로고    scopus 로고
    • Polarized transport of MHC class II molecules in Madin-Darby canine kidney cells is directed by a leucine-based signal in the cytoplasmic tail of the beta-chain
    • Simonsen A, Pedersen KW, Nordeng TW, Von Der Lippe A, Stang E, Long EO, Bakke O (1999b) Polarized transport of MHC class II molecules in Madin-Darby canine kidney cells is directed by a leucine-based signal in the cytoplasmic tail of the beta-chain. J Immunol 163:2540-2548
    • (1999) J Immunol , vol.163 , pp. 2540-2548
    • Simonsen, A.1    Pedersen, K.W.2    Nordeng, T.W.3    Von Der Lippe, A.4    Stang, E.5    Long, E.O.6    Bakke, O.7
  • 318
    • 0029993728 scopus 로고    scopus 로고
    • LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
    • Simske JS, Kaech SM, Harp SA, Kim SK (1996) LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell 85:195-204
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, J.S.1    Kaech, S.M.2    Harp, S.A.3    Kim, S.K.4
  • 319
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner T, Bennett MK, Whiteheart SW, Scheller RH, Rothman JE (1993a) A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75:409-418
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 322
    • 0034520590 scopus 로고    scopus 로고
    • PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
    • Standley S, Roche KW, Mccallum J, Sans N, Wenthold RJ (2000) PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants. Neuron 28:887-898
    • (2000) Neuron , vol.28 , pp. 887-898
    • Standley, S.1    Roche, K.W.2    Mccallum, J.3    Sans, N.4    Wenthold, R.J.5
  • 324
    • 0034617148 scopus 로고    scopus 로고
    • Differential regulation of endogenous cadherin expression in Madin-Darby canine kidney cells by cell-cell adhesion and activation of beta-catenin signaling
    • Stewart DB, Barth AI, Nelson WJ (2000) Differential regulation of endogenous cadherin expression in Madin-Darby canine kidney cells by cell-cell adhesion and activation of beta-catenin signaling. J Biol Chem 275:20707-20716
    • (2000) J Biol Chem , vol.275 , pp. 20707-20716
    • Stewart, D.B.1    Barth, A.I.2    Nelson, W.J.3
  • 325
    • 0029159840 scopus 로고
    • Regulation of vesicular transport by GTP-binding proteins
    • Stow JL (1995) Regulation of vesicular transport by GTP-binding proteins. Curr Opin Nephrol Hypertens 4:421-425
    • (1995) Curr Opin Nephrol Hypertens , vol.4 , pp. 421-425
    • Stow, J.L.1
  • 327
    • 0034757166 scopus 로고    scopus 로고
    • Interaction with mLin-7 alters the targeting of endocytosed transmembrane proteins in mammalian epithelial cells
    • Straight SW, Chen L, Karnak D, Margolis B (2001) Interaction with mLin-7 alters the targeting of endocytosed transmembrane proteins in mammalian epithelial cells. Mol Biol Cell 12:1329-1340
    • (2001) Mol Biol Cell , vol.12 , pp. 1329-1340
    • Straight, S.W.1    Chen, L.2    Karnak, D.3    Margolis, B.4
  • 328
  • 330
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT (1998) Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395:347-353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 331
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A, Yamanaka T, Hirose T, Manabe N, Mizuno K, Shimizu M, Akimoto K, Izumi Y, Ohnishi T, Ohno S (2001) Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J Cell Biol 152:1183-1196
    • (2001) J Cell Biol , vol.152 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 333
    • 0035954436 scopus 로고    scopus 로고
    • Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport
    • Tai AW, Chuang JZ, Sung CH (2001) Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport. J Cell Biol 153:1499-1509
    • (2001) J Cell Biol , vol.153 , pp. 1499-1509
    • Tai, A.W.1    Chuang, J.Z.2    Sung, C.H.3
  • 334
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells
    • Takaishi K, Sasaki T, Kotani H, Nishioka H, Takai Y (1997) Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells. J Cell Biol 139:1047-1059
    • (1997) J Cell Biol , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 335
    • 0037404459 scopus 로고    scopus 로고
    • Identification of an apical sorting determinant in the cytoplasmic tail of megalin
    • Takeda T, Yamazaki H, Farquhar MG (2003) Identification of an apical sorting determinant in the cytoplasmic tail of megalin. Am J Physiol Cell Physiol 284:C1105-1113
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Takeda, T.1    Yamazaki, H.2    Farquhar, M.G.3
  • 336
    • 0037458707 scopus 로고    scopus 로고
    • Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse
    • Takekuni K, Ikeda W, Fujito T, Morimoto K, Takeuchi M, Monden M, Takai Y (2003) Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse. J Biol Chem 278:5497-5500
    • (2003) J Biol Chem , vol.278 , pp. 5497-5500
    • Takekuni, K.1    Ikeda, W.2    Fujito, T.3    Morimoto, K.4    Takeuchi, M.5    Monden, M.6    Takai, Y.7
  • 337
    • 0346752326 scopus 로고    scopus 로고
    • Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL
    • Tall RD, Alonso MA, Roth MG (2004) Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL. Traffic 4:838-849
    • (2004) Traffic , vol.4 , pp. 838-849
    • Tall, R.D.1    Alonso, M.A.2    Roth, M.G.3
  • 338
    • 0037225708 scopus 로고    scopus 로고
    • Interactions between the crumbs, lethal giant larvae and bazooka pathways in epithelial polarization
    • Tanentzapf G, Tepass U (2003) Interactions between the crumbs, lethal giant larvae and bazooka pathways in epithelial polarization. Nat Cell Biol 5:46-52
    • (2003) Nat Cell Biol , vol.5 , pp. 46-52
    • Tanentzapf, G.1    Tepass, U.2
  • 339
    • 0027484630 scopus 로고
    • Crumbs and stardust act in a genetic pathway that controls the organization of epithelia in Drosophila melanogaster
    • Tepass U, Knust E (1993) Crumbs and stardust act in a genetic pathway that controls the organization of epithelia in Drosophila melanogaster. Dev Biol 159:311-326
    • (1993) Dev Biol , vol.159 , pp. 311-326
    • Tepass, U.1    Knust, E.2
  • 340
    • 0025285657 scopus 로고
    • Crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia
    • Tepass U, Theres C, Knust E (1990) crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia. Cell 61:787-799
    • (1990) Cell , vol.61 , pp. 787-799
    • Tepass, U.1    Theres, C.2    Knust, E.3
  • 341
    • 0035674837 scopus 로고    scopus 로고
    • Epithelial cell polarity and cell junctions in Drosophila
    • Tepass U, Tanentzapf G, Ward R, Fehon R (2003) Epithelial cell polarity and cell junctions in Drosophila. Annu Rev Genet 35:747-784
    • (2003) Annu Rev Genet , vol.35 , pp. 747-784
    • Tepass, U.1    Tanentzapf, G.2    Ward, R.3    Fehon, R.4
  • 342
    • 0029843493 scopus 로고    scopus 로고
    • The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • Terbush DR, Maurice T, Roth D, Novick P (1996) The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 15:6483-6994
    • (1996) EMBO J , vol.15 , pp. 6483-6994
    • Terbush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 343
    • 0028217859 scopus 로고
    • The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities
    • Thomas DC, Roth MG (1994) The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities. J Biol Chem 269:15732-15739
    • (1994) J Biol Chem , vol.269 , pp. 15732-15739
    • Thomas, D.C.1    Roth, M.G.2
  • 344
    • 0027407766 scopus 로고
    • Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine
    • Thomas DC, Brewer CB, Roth MG (1993) Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine. J Biol Chem 268:3313-3320
    • (1993) J Biol Chem , vol.268 , pp. 3313-3320
    • Thomas, D.C.1    Brewer, C.B.2    Roth, M.G.3
  • 345
    • 0032896704 scopus 로고    scopus 로고
    • Distribution of postsynaptic density proteins in rat kidney: Relationship to neuronal nitric oxide synthase
    • Tojo A, Bredt DS, Wilcox CS (1999) Distribution of postsynaptic density proteins in rat kidney: Relationship to neuronal nitric oxide synthase. Kidney Int 55:1384-1394
    • (1999) Kidney Int , vol.55 , pp. 1384-1394
    • Tojo, A.1    Bredt, D.S.2    Wilcox, C.S.3
  • 346
    • 0345099309 scopus 로고    scopus 로고
    • AP-1B: Polarized sorting at the endosome
    • Traub LM, Apodaca G (2003) AP-1B: Polarized sorting at the endosome. Nat Cell Biol 5:1045-1047
    • (2003) Nat Cell Biol , vol.5 , pp. 1045-1047
    • Traub, L.M.1    Apodaca, G.2
  • 347
    • 0037817352 scopus 로고    scopus 로고
    • Transcytosis: Crossing cellular barriers
    • Tuma PL, Hubbard AL (2003) Transcytosis: Crossing cellular barriers. Physiol Rev 83:871-932
    • (2003) Physiol Rev , vol.83 , pp. 871-932
    • Tuma, P.L.1    Hubbard, A.L.2
  • 348
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale RD (2003) The molecular motor toolbox for intracellular transport. Cell 112:467-480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 349
    • 0028350154 scopus 로고
    • An induced extracellular matrix protein reverses the polarity of band 3 in intercalated epithelial cells
    • Van Adelsberg J, Edwards JC, Takito J, Kiss B, Al-Awqati Q (1994) An induced extracellular matrix protein reverses the polarity of band 3 in intercalated epithelial cells. Cell 76:1053-1061
    • (1994) Cell , vol.76 , pp. 1053-1061
    • Van Adelsberg, J.1    Edwards, J.C.2    Takito, J.3    Kiss, B.4    Al-Awqati, Q.5
  • 350
    • 0033917216 scopus 로고    scopus 로고
    • The subapical compartment and its role in intracellular trafficking and cell polarity
    • Van Ijzendoorn SCD, Maier O, Van Der Wouden JM, Hoekstra D (2000) The subapical compartment and its role in intracellular trafficking and cell polarity. J Cell Physiol 184:151-160
    • (2000) J Cell Physiol , vol.184 , pp. 151-160
    • Van Ijzendoorn, S.C.D.1    Maier, O.2    Van Der Wouden, J.M.3    Hoekstra, D.4
  • 351
    • 0036480017 scopus 로고    scopus 로고
    • Direct interaction between Rab 3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells
    • Van Ijzendoorn SCD, Tuvim MJ, Weimbs T, Dickey BF, Mostov KE (2002) Direct interaction between Rab 3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells. Dev Cell 2:219-228
    • (2002) Dev Cell , vol.2 , pp. 219-228
    • Van Ijzendoorn, S.C.D.1    Tuvim, M.J.2    Weimbs, T.3    Dickey, B.F.4    Mostov, K.E.5
  • 352
    • 0023198134 scopus 로고
    • Formation of the apical pole of epithelial (Madin-Darby canine kidney) cells: Polarity of an apical protein is independent of tight junctions while segregation of a basolateral marker requires cell-cell interactions
    • Vega-Salas DE, Salas PJ, Gundersen D, Rodriguez-Boulan E (1987a) Formation of the apical pole of epithelial (Madin-Darby canine kidney) cells: Polarity of an apical protein is independent of tight junctions while segregation of a basolateral marker requires cell-cell interactions. J Cell Biol 104:905-916
    • (1987) J Cell Biol , vol.104 , pp. 905-916
    • Vega-Salas, D.E.1    Salas, P.J.2    Gundersen, D.3    Rodriguez-Boulan, E.4
  • 353
    • 0023227132 scopus 로고
    • Modulation of the expression of an apical plasma membrane protein of Madin-Darby canine kidney epithelial cells: Cell-cell interactions control the appearance of a novel intracellular storage compartment
    • Vega-Salas DE, Salas PJ, Rodriguez-Boulan E (1987b) Modulation of the expression of an apical plasma membrane protein of Madin-Darby canine kidney epithelial cells: Cell-cell interactions control the appearance of a novel intracellular storage compartment. J Cell Biol 104:1249-1259
    • (1987) J Cell Biol , vol.104 , pp. 1249-1259
    • Vega-Salas, D.E.1    Salas, P.J.2    Rodriguez-Boulan, E.3
  • 354
    • 0024110256 scopus 로고
    • Exocytosis of vacuolar apical compartment (VAC): A cell-cell contact controlled mechanism for the establishment of the apical plasma membrane domain in epithelial cells
    • Vega-Salas DE, Salas PJ, Rodriguez-Boulan E (1988) Exocytosis of vacuolar apical compartment (VAC): A cell-cell contact controlled mechanism for the establishment of the apical plasma membrane domain in epithelial cells. J Cell Biol 107:1717-1728
    • (1988) J Cell Biol , vol.107 , pp. 1717-1728
    • Vega-Salas, D.E.1    Salas, P.J.2    Rodriguez-Boulan, E.3
  • 355
    • 0031229420 scopus 로고    scopus 로고
    • Robert Feulgen Lecture 1997. Lipid microdomains and membrane trafficking in mammalian cells
    • Verkade P, Simons K (1997) Robert Feulgen Lecture 1997. Lipid microdomains and membrane trafficking in mammalian cells. Histochem Cell Biol 108:211-220
    • (1997) Histochem Cell Biol , vol.108 , pp. 211-220
    • Verkade, P.1    Simons, K.2
  • 356
    • 0031980371 scopus 로고    scopus 로고
    • Expression of caveolin-1 and polarized formation of invaginated caveolae in Caco-2 and MDCK II cells
    • Vogel U, Sandvig K, Van Deurs B (1998) Expression of caveolin-1 and polarized formation of invaginated caveolae in Caco-2 and MDCK II cells. J Cell Sci 111:825-832
    • (1998) J Cell Sci , vol.111 , pp. 825-832
    • Vogel, U.1    Sandvig, K.2    Van Deurs, B.3
  • 357
    • 0022154174 scopus 로고
    • Apical and basolateral endocytosis in Madin-Darby canine kidney (MDCK) cells grown on nitrocellulose filters
    • Von Bonsdorff CH, Fuller SD, Simons K (1985) Apical and basolateral endocytosis in Madin-Darby canine kidney (MDCK) cells grown on nitrocellulose filters. EMBO J 4:2781-2792
    • (1985) EMBO J , vol.4 , pp. 2781-2792
    • Von Bonsdorff, C.H.1    Fuller, S.D.2    Simons, K.3
  • 359
    • 0029058691 scopus 로고
    • The oligosaccharides have an essential but indirect role in sorting gp80 (clusterin, TRPM-2) to the apical surface of MDCK cells
    • Wagner M, Morgans C, Koch-Brandt C (1995) The oligosaccharides have an essential but indirect role in sorting gp80 (clusterin, TRPM-2) to the apical surface of MDCK cells. Eur J Cell Biol 67:84-88
    • (1995) Eur J Cell Biol , vol.67 , pp. 84-88
    • Wagner, M.1    Morgans, C.2    Koch-Brandt, C.3
  • 360
    • 0026716393 scopus 로고
    • Brefeldin A enhances receptor-mediated transcytosis of transferrin in filter-grown Madin-Darby canine kidney cells
    • Wan J, Taub ME, Shah D, Shen WC (1992) Brefeldin A enhances receptor-mediated transcytosis of transferrin in filter-grown Madin-Darby canine kidney cells. J Biol Chem 267:13446-13450
    • (1992) J Biol Chem , vol.267 , pp. 13446-13450
    • Wan, J.1    Taub, M.E.2    Shah, D.3    Shen, W.C.4
  • 361
    • 0025153020 scopus 로고
    • Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells
    • Wandinger-Ness A, Bennett MK, Antony C, Simons K (1990) Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells. J Cell Biol 111:987-1000
    • (1990) J Cell Biol , vol.111 , pp. 987-1000
    • Wandinger-Ness, A.1    Bennett, M.K.2    Antony, C.3    Simons, K.4
  • 362
    • 0025023525 scopus 로고
    • Steps in the morphogenesis of a polarized epithelium. I. Uncoupling the roles of cell-cell and cell-substratum contact in establishing plasma membrane polarity in multicellular epithelial (MDCK) cysts
    • Wang AZ, Ojakian GK, Nelson WJ (1990a) Steps in the morphogenesis of a polarized epithelium. I. Uncoupling the roles of cell-cell and cell-substratum contact in establishing plasma membrane polarity in multicellular epithelial (MDCK) cysts. J Cell Sci 95:137-151
    • (1990) J Cell Sci , vol.95 , pp. 137-151
    • Wang, A.Z.1    Ojakian, G.K.2    Nelson, W.J.3
  • 363
    • 0025191452 scopus 로고
    • Steps in the morphogenesis of a polarized epithelium. II. Disassembly and assembly of plasma membrane domains during reversal of epithelial cell polarity in multicellular epithelial (MDCK) cysts
    • Wang AZ, Ojakian GK, Nelson WJ (1990b) Steps in the morphogenesis of a polarized epithelium. II. Disassembly and assembly of plasma membrane domains during reversal of epithelial cell polarity in multicellular epithelial (MDCK) cysts. J Cell Sci 95:153-165
    • (1990) J Cell Sci , vol.95 , pp. 153-165
    • Wang, A.Z.1    Ojakian, G.K.2    Nelson, W.J.3
  • 364
    • 0034208649 scopus 로고    scopus 로고
    • Apical and basolateral endocytic pathways of MDCK cells meet in acidic common endosomes distinct from a nearly neutral apical recycling endosome
    • Wang E, Brown PS, Aroeti B, Chapin SJ, Mostov KE, Dunn KW (2000) Apical and basolateral endocytic pathways of MDCK cells meet in acidic common endosomes distinct from a nearly neutral apical recycling endosome. Traffic 1:480-493
    • (2000) Traffic , vol.1 , pp. 480-493
    • Wang, E.1    Brown, P.S.2    Aroeti, B.3    Chapin, S.J.4    Mostov, K.E.5    Dunn, K.W.6
  • 365
    • 0034773182 scopus 로고    scopus 로고
    • Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells
    • Wang E, Pennington JG, Goldenring JR, Hunziker W, Dunn KW (2002) Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells. J Cell Sci 114:3309-3321
    • (2002) J Cell Sci , vol.114 , pp. 3309-3321
    • Wang, E.1    Pennington, J.G.2    Goldenring, J.R.3    Hunziker, W.4    Dunn, K.W.5
  • 366
    • 0032080043 scopus 로고    scopus 로고
    • Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of CFTR
    • Wang S, Raab RW, Schatz PJ, Guggino WB, Li M (1998) Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of CFTR. FEBS Lett 427:103-108
    • (1998) FEBS Lett , vol.427 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5
  • 367
    • 0034730330 scopus 로고    scopus 로고
    • Accessory protein facilitated CFTR-CFTR interaction a molecular mechanism to potentiate the chloride channel activity
    • Wang S, Yue H, Derin RB, Guggino WB, Li M (2001) Accessory protein facilitated CFTR-CFTR interaction a molecular mechanism to potentiate the chloride channel activity. Cell 103:169-179
    • (2001) Cell , vol.103 , pp. 169-179
    • Wang, S.1    Yue, H.2    Derin, R.B.3    Guggino, W.B.4    Li, M.5
  • 368
    • 0034666356 scopus 로고    scopus 로고
    • Regulation of vesicle trafficking in Madin-Darby canine kidney cells by Rab 11a and Rab 25
    • Wang X, Kumar R, Navarre J, Casanova JE, Goldenring JR (2000) Regulation of vesicle trafficking in Madin-Darby canine kidney cells by Rab 11a and Rab 25. J Biol Chem 275:29138-29146
    • (2000) J Biol Chem , vol.275 , pp. 29138-29146
    • Wang, X.1    Kumar, R.2    Navarre, J.3    Casanova, J.E.4    Goldenring, J.R.5
  • 369
    • 0033179888 scopus 로고    scopus 로고
    • Membrane tethering in intracellular transport
    • Waters MG, Pfeffer SR (1999) Membrane tethering in intracellular transport. Curr Opin Cell Biol 11:453-459
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 453-459
    • Waters, M.G.1    Pfeffer, S.R.2
  • 370
    • 0035918242 scopus 로고    scopus 로고
    • Stem cell factor presentation to c-Kit. Identification of a basolateral targeting domain
    • Wehrle-Haller B, Imhof BA (2001) Stem cell factor presentation to c-Kit. Identification of a basolateral targeting domain. J Biol Chem 276:12667-12674
    • (2001) J Biol Chem , vol.276 , pp. 12667-12674
    • Wehrle-Haller, B.1    Imhof, B.A.2
  • 373
    • 0033840979 scopus 로고    scopus 로고
    • EEA1 a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts
    • Wilson JM, De Hoop M, Zorzi N, Toh BH, Dotti CG, Parton RG (2000) EEA1 a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts. Mol Biol Cell 11:2657-2671
    • (2000) Mol Biol Cell , vol.11 , pp. 2657-2671
    • Wilson, J.M.1    De Hoop, M.2    Zorzi, N.3    Toh, B.H.4    Dotti, C.G.5    Parton, R.G.6
  • 374
    • 0029045343 scopus 로고
    • Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila
    • Wodarz A, Hinz U, Engelbert M, Knust E (1995) Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila. Cell 82:67-76
    • (1995) Cell , vol.82 , pp. 67-76
    • Wodarz, A.1    Hinz, U.2    Engelbert, M.3    Knust, E.4
  • 375
    • 0031694195 scopus 로고    scopus 로고
    • Subcellular targeting and cytoskeletal attachment of SAP97 to the epithelial lateral membrane
    • Wu H, Reuver SM, Kuhlendahl S, Chung WJ, Garner CC (1998) Subcellular targeting and cytoskeletal attachment of SAP97 to the epithelial lateral membrane. J Cell Sci 111:2365-2376
    • (1998) J Cell Sci , vol.111 , pp. 2365-2376
    • Wu, H.1    Reuver, S.M.2    Kuhlendahl, S.3    Chung, W.J.4    Garner, C.C.5
  • 376
    • 0032572532 scopus 로고    scopus 로고
    • Coordination of an array of signaling proteins through homo- and heteromeric interactions between PDZ domains and target proteins
    • Xu XZ, Choudhury A, Li X, Montell C (1998) Coordination of an array of signaling proteins through homo- and heteromeric interactions between PDZ domains and target proteins. J Cell Biol 142:545-555
    • (1998) J Cell Biol , vol.142 , pp. 545-555
    • Xu, X.Z.1    Choudhury, A.2    Li, X.3    Montell, C.4
  • 378
  • 379
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells
    • Yeaman C, Le Gall AH, Baldwin AN, Monlauzeur L, Le Bivic A, Rodriguez-Boulan E (1997) The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J Cell Biol 139:929-940
    • (1997) J Cell Biol , vol.139 , pp. 929-940
    • Yeaman, C.1    Le Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Le Bivic, A.5    Rodriguez-Boulan, E.6
  • 380
    • 0032956497 scopus 로고    scopus 로고
    • New perspectives on mechanisms involved in generating epithelial cell polarity
    • Yeaman C, Grindstaff KK, Nelson WJ (1999) New perspectives on mechanisms involved in generating epithelial cell polarity. Physiol Rev 79:73-98
    • (1999) Physiol Rev , vol.79 , pp. 73-98
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3
  • 381
    • 0035969243 scopus 로고    scopus 로고
    • Sec 6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells
    • Yeaman C, Grindstaff KK, Wright JR, Nelson WJ (2001) Sec 6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells. J Cell Biol 155:593-604
    • (2001) J Cell Biol , vol.155 , pp. 593-604
    • Yeaman, C.1    Grindstaff, K.K.2    Wright, J.R.3    Nelson, W.J.4
  • 385
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor
    • Zhu Y, Doray B, Poussu A, Lehto VP, Kornfeld S (2001) Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science 292:1716-1718
    • (2001) Science , vol.292 , pp. 1716-1718
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.P.4    Kornfeld, S.5
  • 386
    • 0027315413 scopus 로고
    • Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells
    • Zurzolo C, Lisanti MP, Caras IW, Nitsch L, Rodriguez-Boulan E (1993) Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells. J Cell Biol 121:1031-1039
    • (1993) J Cell Biol , vol.121 , pp. 1031-1039
    • Zurzolo, C.1    Lisanti, M.P.2    Caras, I.W.3    Nitsch, L.4    Rodriguez-Boulan, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.