메뉴 건너뛰기




Volumn 9, Issue 5, 1998, Pages 503-509

Protein and lipid sorting from the trans-Golgi network to the plasma membrane in polarized cells

Author keywords

Epithelial cell; Lipid and protein transport; Sorting signal membrane raft

Indexed keywords

CHOLESTEROL; GLYCOSPHINGOLIPID; MEMBRANE LIPID; MEMBRANE PROTEIN; POLYSACCHARIDE; SIGNAL PEPTIDE;

EID: 0032177419     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1998.0258     Document Type: Article
Times cited : (154)

References (73)
  • 1
    • 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
  • 2
    • 0027902050 scopus 로고
    • Biogenesis of epithelial cell surface polarity
    • Simons K (1995) Biogenesis of epithelial cell surface polarity. Harvey Lect 89:125-146
    • (1995) Harvey Lect , vol.89 , pp. 125-146
    • Simons, K.1
  • 3
    • 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
  • 4
    • 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
  • 5
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387:569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 6
    • 0029998349 scopus 로고    scopus 로고
    • Cell-specific sorting of biogenic amine transporters expressed in epthelial cells
    • Gu HH, Ahn J, Caplan MJ, Blakely RD, Levey AI, Rudnick G (1996) Cell-specific sorting of biogenic amine transporters expressed in epthelial cells. J Biol Chem 271:18100-18106
    • (1996) J Biol Chem , vol.271 , pp. 18100-18106
    • Gu, H.H.1    Ahn, J.2    Caplan, M.J.3    Blakely, R.D.4    Levey, A.I.5    Rudnick, G.6
  • 7
    • 0029780812 scopus 로고    scopus 로고
    • Two different cytoplasmic tails direct isoforms of the membrane cofactor protein (CD46) to the basolateral surface of Madin-Darby canine kidney cells
    • Maisner A, Liszewski MK, Atkinson JP, Schwartz-Albiez R, Herrler G (1996) Two different cytoplasmic tails direct isoforms of the membrane cofactor protein (CD46) to the basolateral surface of Madin-Darby canine kidney cells. J Biol Chem 271:18853-18858
    • (1996) J Biol Chem , vol.271 , pp. 18853-18858
    • Maisner, A.1    Liszewski, M.K.2    Atkinson, J.P.3    Schwartz-Albiez, R.4    Herrler, G.5
  • 8
    • 0030755820 scopus 로고    scopus 로고
    • Apical sorting of influenza hemagglutinin by transcytosis in retinal pigment epithelium
    • Bonilha VL, Marmorstein AD, Cohen-Gould L, Rodriguez-Boulan E (1997) Apical sorting of influenza hemagglutinin by transcytosis in retinal pigment epithelium. J Cell Sci 110:1717-1727
    • (1997) J Cell Sci , vol.110 , pp. 1717-1727
    • Bonilha, V.L.1    Marmorstein, A.D.2    Cohen-Gould, L.3    Rodriguez-Boulan, E.4
  • 9
    • 0026579206 scopus 로고
    • Modulation of transcytotic and direct targeting pathways in a polarized thyroid cell line
    • Zurzolo C, Le Bivic A, Quaroni A, Nitsch L, Rodriguez-Boulan E (1992) Modulation of transcytotic and direct targeting pathways in a polarized thyroid cell line. EMBO J 11:2337-2344
    • (1992) EMBO J , vol.11 , pp. 2337-2344
    • Zurzolo, C.1    Le Bivic, A.2    Quaroni, A.3    Nitsch, L.4    Rodriguez-Boulan, E.5
  • 11
    • 0029852842 scopus 로고    scopus 로고
    • Hensin, a new collecting duct protein involved in the in vitro plasticity of intercalated cell polarity
    • Takito J, Hikita C, Al-Awqati Q (1996) Hensin, a new collecting duct protein involved in the in vitro plasticity of intercalated cell polarity. J Clin Invest 98:2324-2331
    • (1996) J Clin Invest , vol.98 , pp. 2324-2331
    • Takito, J.1    Hikita, C.2    Al-Awqati, Q.3
  • 12
    • 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
  • 13
    • 0030838739 scopus 로고    scopus 로고
    • Membrane cofactor protein (CD46) is a basolateral protein that is not endocytosed. Importance of the tetrapeptide FTSL at the acrboxyl terminus
    • Maisner A, Zimmer G, Liszewski MK, Lublin DM, Atkinson JP, Herrler G (1997) Membrane cofactor protein (CD46) is a basolateral protein that is not endocytosed. Importance of the tetrapeptide FTSL at the acrboxyl terminus. J Biol Chem 272:20793-20799
    • (1997) J Biol Chem , vol.272 , pp. 20793-20799
    • Maisner, A.1    Zimmer, G.2    Liszewski, M.K.3    Lublin, D.M.4    Atkinson, J.P.5    Herrler, G.6
  • 14
    • 0030941972 scopus 로고    scopus 로고
    • Sorting of two polytopic proteins, the γ-aminobutyric acid betaine transporters, in polarized epithelial cells
    • Perego C, Bulbarelli A, Longhi R et al (1997) Sorting of two polytopic proteins, the γ-aminobutyric acid 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
  • 15
    • 0031972754 scopus 로고    scopus 로고
    • Basolateral sorting of the cation-dependent mannose 6-phosphate receptor in Madin-Darby canine kidney cells. Identification of a basolateral determinant unrelated to clathrin-coated pit localization signals
    • Distel B, Bauer U, Le Borgne R, Hoflack B (1998) Basolateral sorting of the cation-dependent mannose 6-phosphate receptor in Madin-Darby canine kidney cells. Identification of a basolateral determinant unrelated to clathrin-coated pit localization signals. J Biol Chem 273:186-193
    • (1998) J Biol Chem , vol.273 , pp. 186-193
    • Distel, B.1    Bauer, U.2    Le Borgne, R.3    Hoflack, B.4
  • 16
    • 0032563306 scopus 로고    scopus 로고
    • PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization
    • Wan L, Molloy SS, Thomas L et al (1998) PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization. Cell 94:205-216
    • (1998) Cell , vol.94 , pp. 205-216
    • Wan, L.1    Molloy, S.S.2    Thomas, L.3
  • 17
    • 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
  • 18
    • 0032544535 scopus 로고    scopus 로고
    • Sorting out genes that regulate epithelial and neuronal polarity
    • Bredt DS (1998) Sorting out genes that regulate epithelial and neuronal polarity. Cell 94:691-694
    • (1998) Cell , vol.94 , pp. 691-694
    • Bredt, D.S.1
  • 19
    • 0023267654 scopus 로고
    • Modulation of fodrin (membrane skeleton) stability by cell-cell contact in Madin-Darby canine kidney epithelial cells
    • Nelson WJ, Veshnock PJ (1987) Modulation of fodrin (membrane skeleton) stability by cell-cell contact in Madin-Darby canine kidney epithelial cells. J Cell Biol 104:1527-1537
    • (1987) J Cell Biol , vol.104 , pp. 1527-1537
    • Nelson, W.J.1    Veshnock, P.J.2
  • 20
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown RE (1998) Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J Cell Sci 111:1-9
    • (1998) J Cell Sci , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 21
    • 0031558768 scopus 로고    scopus 로고
    • Structure of detergent-resistant membrane domains: Does phase separation occur in biological membranes?
    • Brown DA, London E (1997) Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes? Biochem Biophys Res Commun 240:1-7
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 1-7
    • Brown, D.A.1    London, E.2
  • 22
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • in press
    • Rietveld A, Simons K (1998) The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim Biophys Acta in press
    • (1998) Biochim Biophys Acta
    • Rietveld, A.1    Simons, K.2
  • 23
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T, Kurzchalia TV (1998) Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394:802-805
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 24
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S (1998) GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394:798-801
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 25
    • 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
  • 26
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl-phosphatidyl-anchored protein targeting to a glycolipid-enriched membrane fraction
    • Rodgers W, Crise B, Rose JK (1994) Signals determining protein tyrosine kinase and glycosyl-phosphatidyl-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol Cell Biol 14:5384-5391
    • (1994) Mol Cell Biol , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 27
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele P, Roth MG, Simons K (1997) Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J 16:5501-5508
    • (1997) EMBO J , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 28
    • 0028173679 scopus 로고
    • The fats of the matter
    • Resh MD (1994) The fats of the matter. Cell 76:411-413
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 29
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey PJ (1995) Protein lipidation in cell signaling. Science 268:221-224
    • (1995) Science , vol.268 , pp. 221-224
    • Casey, P.J.1
  • 30
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T, Scheiffele P, Verkade P, Simons K (1998) Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol 141:929-942
    • (1998) J Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 31
    • 15844386540 scopus 로고    scopus 로고
    • Hedgehog patterning activity: Role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain
    • Porter JA, Ekker SC, Park W-J et al (1996) Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain. Cell 86:21-34
    • (1996) Cell , vol.86 , pp. 21-34
    • Porter, J.A.1    Ekker, S.C.2    Park, W.-J.3
  • 32
    • 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
  • 33
    • 0026447375 scopus 로고
    • Effects of altering palmitoylation sites on biosynthesis and function of the influenza virus hemagglutinin
    • Naim HY, Amarneh B, Ktistakis NT, Roth MG (1992) Effects of altering palmitoylation sites on biosynthesis and function of the influenza virus hemagglutinin. J Virol 66:7585-7588
    • (1992) J Virol , vol.66 , pp. 7585-7588
    • Naim, H.Y.1    Amarneh, B.2    Ktistakis, N.T.3    Roth, M.G.4
  • 34
    • 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
  • 35
    • 0032055472 scopus 로고    scopus 로고
    • Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins
    • Gut A, Kappeler F, Hyka N, Balda MS, Hauri H-P, Matter K (1998) Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins. EMBO J 17:1919-1929
    • (1998) EMBO J , vol.17 , pp. 1919-1929
    • Gut, A.1    Kappeler, F.2    Hyka, N.3    Balda, M.S.4    Hauri, H.-P.5    Matter, K.6
  • 36
    • 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
  • 37
    • 0032526691 scopus 로고    scopus 로고
    • GalNAc-α-O-benzyl inhibits NeuAcα2-3 glycosylation and blocks the intracellular transport of apical glycoproteins and mucus in differentiated HT-29 cells
    • Huet G, Hennebicq-Reig S, De Bolos C et al (1998) GalNAc-α-O-benzyl inhibits NeuAcα2-3 glycosylation and blocks the intracellular transport of apical glycoproteins and mucus in differentiated HT-29 cells. J Cell Biol 141:1311-1322
    • (1998) J Cell Biol , vol.141 , pp. 1311-1322
    • Huet, G.1    Hennebicq-Reig, S.2    De Bolos, C.3
  • 38
    • 0030051122 scopus 로고    scopus 로고
    • Characterization of VIP36, an animal lectin homologous to leguminous lectins
    • Fiedler K, Simons K (1996) Characterization of VIP36, an animal lectin homologous to leguminous lectins. J Cell Sci 109:271-276
    • (1996) J Cell Sci , vol.109 , pp. 271-276
    • Fiedler, K.1    Simons, K.2
  • 39
    • 0032478548 scopus 로고    scopus 로고
    • Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII
    • Nichols WC, Seligsohn U, Zivelin A et al (1998) Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII. Cell 93:61-70
    • (1998) Cell , vol.93 , pp. 61-70
    • Nichols, W.C.1    Seligsohn, U.2    Zivelin, A.3
  • 40
    • 0032572579 scopus 로고    scopus 로고
    • Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme
    • Vollenweider F, Rappeler F, Itin C, Hauri H-P (1998) Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme. J Cell Biol 142:377-389
    • (1998) J Cell Biol , vol.142 , pp. 377-389
    • Vollenweider, F.1    Rappeler, F.2    Itin, C.3    Hauri, H.-P.4
  • 41
    • 0032494121 scopus 로고    scopus 로고
    • The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells
    • Chuang J-Z, Sung C-H (1998) The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells. J Cell Biol 142:1245-1256
    • (1998) J Cell Biol , vol.142 , pp. 1245-1256
    • Chuang, J.-Z.1    Sung, C.-H.2
  • 42
    • 0025913946 scopus 로고
    • A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin
    • Brewer CB, Roth MG (1991) A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J Cell Biol 114:413-421
    • (1991) J Cell Biol , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 43
    • 0028069680 scopus 로고
    • Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins
    • Kundu A, Nayak DP (1994) Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins. J Virol 68:1812-1818
    • (1994) J Virol , vol.68 , pp. 1812-1818
    • Kundu, A.1    Nayak, D.P.2
  • 44
    • 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
  • 45
    • 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
  • 47
    • 0032559560 scopus 로고    scopus 로고
    • Caveolin-1 and -2 in the exocytic pathway of MDCK cells
    • Scheiffele P, Verkade, Fra M, Virta, Simons, Ikonen (1998) Caveolin-1 and -2 in the exocytic pathway of MDCK cells. J Cell Biol 140:795-806
    • (1998) J Cell Biol , vol.140 , pp. 795-806
    • Scheiffele, P.1    Verkade2    Fra, M.3    Virta4    Simons5    Ikonen6
  • 48
    • 0030940183 scopus 로고    scopus 로고
    • Myelin and lymphocyte protein (MAL/MVP17/VIP17) and plasmolipin are members of an extended gene family
    • Magyar JP, Ebensperger C, Schaeren-Wiemers N, Suter U (1997) Myelin and lymphocyte protein (MAL/MVP17/VIP17) and plasmolipin are members of an extended gene family. Gene 189:269-275
    • (1997) Gene , vol.189 , pp. 269-275
    • Magyar, J.P.1    Ebensperger, C.2    Schaeren-Wiemers, N.3    Suter, U.4
  • 49
    • 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
  • 51
    • 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
  • 52
    • 0030780090 scopus 로고    scopus 로고
    • Molecular motors and a spectrin matrix associate with Golgi membranes in vitro
    • Fath KR, Trimbur GM, Burgess DR (1997) Molecular motors and a spectrin matrix associate with Golgi membranes in vitro. J Cell Biol 139:1169-1181
    • (1997) J Cell Biol , vol.139 , pp. 1169-1181
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 53
    • 0028969528 scopus 로고
    • Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface
    • Futter CE, Connolly CN, Cutler DF, Hopkins CR (1995) Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface. J Biol Chem 270:10999-11003
    • (1995) J Biol Chem , vol.270 , pp. 10999-11003
    • Futter, C.E.1    Connolly, C.N.2    Cutler, D.F.3    Hopkins, C.R.4
  • 54
    • 0029935911 scopus 로고    scopus 로고
    • In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting
    • Heilker R, Manning-Krieg U, Zuber J-F, Spiess M (1996) In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. EMBO J 15:2893-2899
    • (1996) EMBO J , vol.15 , pp. 2893-2899
    • Heilker, R.1    Manning-Krieg, U.2    Zuber, J.-F.3    Spiess, M.4
  • 55
    • 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
  • 56
    • 0029819793 scopus 로고    scopus 로고
    • Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts
    • Peranen J, Auvinen P, Virta H, Wepf R, Simons K (1996) Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts. J Cell Biol 135:153-167
    • (1996) J Cell Biol , vol.135 , pp. 153-167
    • Peranen, J.1    Auvinen, P.2    Virta, H.3    Wepf, R.4    Simons, K.5
  • 57
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 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 et al (1998) Sec6/8 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
  • 58
    • 0031852067 scopus 로고    scopus 로고
    • Spatial regulation of exocytosis: Lessons from yeast
    • Finger FP, Novick P (1998) Spatial regulation of exocytosis: lessons from yeast. J Cell Biol 142:609-612
    • (1998) J Cell Biol , vol.142 , pp. 609-612
    • Finger, F.P.1    Novick, P.2
  • 59
    • 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
  • 60
    • 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 et al (1998) A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol Biol Cell 9:1437-1448
    • (1998) Mol Biol Cell , vol.9 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3
  • 61
    • 0000777226 scopus 로고    scopus 로고
    • The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells
    • Low SH, Chapin SJ, Wimmer C et al (1998) The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells. J Cell Biol 141:1503-1513
    • (1998) J Cell Biol , vol.141 , pp. 1503-1513
    • Low, S.H.1    Chapin, S.J.2    Wimmer, C.3
  • 63
    • 0030989930 scopus 로고    scopus 로고
    • Identification of detergent-resistant plasma membrane microdomains in Dictyostelium: Enrichment of signal transduction proteins
    • Xiao Z, Devreotes PN (1997) Identification of detergent-resistant plasma membrane microdomains in Dictyostelium: enrichment of signal transduction proteins. Mol Biol Cell 8:855-869
    • (1997) Mol Biol Cell , vol.8 , pp. 855-869
    • Xiao, Z.1    Devreotes, P.N.2
  • 64
    • 0025361892 scopus 로고
    • Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture
    • Dotti CG, Simons K (1990) Polarized sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons in culture. Cell 62:63-72
    • (1990) Cell , vol.62 , pp. 63-72
    • Dotti, C.G.1    Simons, K.2
  • 66
    • 0032584212 scopus 로고    scopus 로고
    • Neuronal polarity: Essential role of protein-lipid complexes in axonal sorting
    • Ledesma MD, Simons K, Dotti CG (1998) Neuronal polarity: essential role of protein-lipid complexes in axonal sorting. Proc Natl Acad Sci USA 95:3966-3971
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3966-3971
    • Ledesma, M.D.1    Simons, K.2    Dotti, C.G.3
  • 67
    • 0032498607 scopus 로고    scopus 로고
    • Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons
    • Nakata T, Terada S, Hirokawa N (1998) Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons. J Cell Biol 140:659-674
    • (1998) J Cell Biol , vol.140 , pp. 659-674
    • Nakata, T.1    Terada, S.2    Hirokawa, N.3
  • 68
    • 0028885854 scopus 로고
    • GMl-gang-lioside-bound amyloid beta-protein (A beta): A possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K, Odaka A, Suzuki N, Ihara Y (1995) GMl-gang-lioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease. Nat Med 1:1062-1066
    • (1995) Nat Med , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 71
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos A, Scott M, Semenov A et al (1995) Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J Cell Biol 129:121-132
    • (1995) J Cell Biol , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3
  • 72
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky N, Stein R, Yanai A, Friedlander G, Taraboulos A (1997) Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J Biol Chem 272:6324-6331
    • (1997) J Biol Chem , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 73
    • 0027976761 scopus 로고
    • The Niemann-Pick C lesion and its relationship to the intracellular distribution and utilization of LDL cholesterol
    • Pentchev PG, Brady RO, Blanchette-Mackie EJ et al (1994) The Niemann-Pick C lesion and its relationship to the intracellular distribution and utilization of LDL cholesterol. Biochim Biophys Acta 1225:235-243
    • (1994) Biochim Biophys Acta , vol.1225 , pp. 235-243
    • Pentchev, P.G.1    Brady, R.O.2    Blanchette-Mackie, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.