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Volumn 226, Issue , 2003, Pages 127-164

Membrane dynamics and the regulation of epithelial cell polarity

Author keywords

Cell polarity; Epithelial cells; Membrane domains; Membrane trafficking; Tight junctions

Indexed keywords

ANIMAL; CELL ADHESION; CELL COMMUNICATION; CELL COMPARTMENTALIZATION; CELL MEMBRANE; CELL POLARITY; CYTOLOGY; ENDOCYTOSIS; ENDOSOME; EPITHELIUM CELL; HUMAN; MEMBRANE TRANSPORT; MOLECULAR DYNAMICS; NONHUMAN; PHYSIOLOGY; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION; TIGHT JUNCTION;

EID: 0043072818     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(03)01003-9     Document Type: Article
Times cited : (26)

References (186)
  • 1
    • 0037010173 scopus 로고    scopus 로고
    • Sphingolipid trafficking and protein sorting in epithelial cells
    • Aït Slimane, T., and Hoekstra, D. (2002). Sphingolipid trafficking and protein sorting in epithelial cells. FEBS Lett. 529, 54-59.
    • (2002) FEBS Lett. , vol.529 , pp. 54-59
    • Aït Slimane, T.1    Hoekstra, D.2
  • 2
    • 0037323554 scopus 로고    scopus 로고
    • Raft-medicated trafficking of apical resident protein occurs in both direct and trancycotic pathways in polarized hepatic cells: Role of distinct lipid microdomains
    • Aït Slimane, T. A., Trujuan, G., van IJendoorn, S. C. D., and Hoekstra, D. (2003). Raft-medicated trafficking of apical resident protein occurs in both direct and trancycotic pathways in polarized hepatic cells: Role of distinct lipid microdomains. Mol. Biol. Cells 14, 620-624.
    • (2003) Mol. Biol. Cells , vol.14 , pp. 620-624
    • Aït Slimane, T.A.1    Trujuan, G.2    Van IJendoorn, S.C.D.3    Hoekstra, D.4
  • 3
    • 0035158750 scopus 로고    scopus 로고
    • RAC1 regulates adherens junctions through endocytosis of E-cadherin
    • Akhtar, N., and Hotchin, N. A. (2001). RAC1 regulates adherens junctions through endocytosis of E-cadherin. Mol. Biol. Cell 12, 847-862.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 847-862
    • Akhtar, N.1    Hotchin, N.A.2
  • 4
    • 0033519624 scopus 로고    scopus 로고
    • O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts
    • Alfalah, M., Jacob, R., Preuss, U., Zimmer, K. P., Naim, H., and Naim, H. Y. (1999). O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts. Curr. Biol. 9, 593-596.
    • (1999) Curr. Biol. , vol.9 , pp. 593-596
    • Alfalah, M.1    Jacob, R.2    Preuss, U.3    Zimmer, K.P.4    Naim, H.5    Naim, H.Y.6
  • 5
    • 0033523770 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 and endocytosis at the apical surface of Madin-Darby canine kidney cells
    • Altschuler, Y., Liu, S., Katz, L., Tang, K., Hardy, S., Brodsky, F., Apodaca, G., and Mostov, K. (1999). ADP-ribosylation factor 6 and endocytosis at the apical surface of Madin-Darby canine kidney cells. J. Cell Biol. 147, 7-12.
    • (1999) J. Cell Biol. , vol.147 , pp. 7-12
    • Altschuler, Y.1    Liu, S.2    Katz, L.3    Tang, K.4    Hardy, S.5    Brodsky, F.6    Apodaca, G.7    Mostov, K.8
  • 6
    • 0032941962 scopus 로고    scopus 로고
    • Differential behavior of E-cadherin and occludin in their colocalization with ZO-1 during the establishment of epithelial cell polarity
    • Ando-Akatsuka, Y., Yonemura, S., Itoh, M., Furuse, M., and Tsukita, S. (1999). Differential behavior of E-cadherin and occludin in their colocalization with ZO-1 during the establishment of epithelial cell polarity. J. Cell Physiol. 179, 115-125.
    • (1999) J. Cell Physiol. , vol.179 , pp. 115-125
    • Ando-Akatsuka, Y.1    Yonemura, S.2    Itoh, M.3    Furuse, M.4    Tsukita, S.5
  • 7
    • 0025936556 scopus 로고
    • The polymeric immunoglobulin receptor. A model protein to study transcytosis
    • Apodaca, G., Bomsel, M., Arden, J., Breitfeld, P. P., Tang, K., and Mostov, K. E. (1991). The polymeric immunoglobulin receptor. A model protein to study transcytosis. J. Clin. Invest. 87, 1877-1882.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1877-1882
    • Apodaca, G.1    Bomsel, M.2    Arden, J.3    Breitfeld, P.P.4    Tang, K.5    Mostov, K.E.6
  • 8
    • 0030454535 scopus 로고    scopus 로고
    • Formation of nascent secretory vesicles from the trans-Golgi network of endocrine cells is inhibited by tyrosine kinase and phosphatase inhibitors
    • Austin, C. D., and Shields, D. (1996). Formation of nascent secretory vesicles from the trans-Golgi network of endocrine cells is inhibited by tyrosine kinase and phosphatase inhibitors. J. Cell Biol. 135, 1471-1483.
    • (1996) J. Cell Biol. , vol.135 , pp. 1471-1483
    • Austin, C.D.1    Shields, D.2
  • 9
    • 0030835887 scopus 로고    scopus 로고
    • Mitotic phosphorylation of rab4 prevents binding to a specific receptor on endosome membranes
    • Ayad, N., Hull, M., and Mellman, I. (1997). Mitotic phosphorylation of rab4 prevents binding to a specific receptor on endosome membranes. EMBO J. 16, 4497-4507.
    • (1997) EMBO J. , vol.16 , pp. 4497-4507
    • Ayad, N.1    Hull, M.2    Mellman, I.3
  • 10
    • 0028209882 scopus 로고
    • Transport of biosynthetic sphingolipids from Golgi to plasma membrane in HT29 cells: Involvement of different carrier vesicle populations
    • Babia, T., Kok, J. W., van der Haar, M., Kalicharan, R., and Hoekstra, D. (1994). Transport of biosynthetic sphingolipids from Golgi to plasma membrane in HT29 cells: Involvement of different carrier vesicle populations. Eur. J. Cell Biol. 63, 172-181.
    • (1994) Eur. J. Cell Biol. , vol.63 , pp. 172-181
    • Babia, T.1    Kok, J.W.2    Van der Haar, M.3    Kalicharan, R.4    Hoekstra, D.5
  • 11
    • 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, E. H., and 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
  • 12
    • 0031952083 scopus 로고    scopus 로고
    • Tight junctions
    • Balda, M. S., and Matter, K. (1998). Tight junctions. J. Cell Sci. 111, 541-547.
    • (1998) J. Cell Sci. , vol.111 , pp. 541-547
    • Balda, M.S.1    Matter, K.2
  • 13
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda, M. S., and Matter, K. (2000). The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J. 19, 2024-2033.
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 15
    • 0036153912 scopus 로고    scopus 로고
    • Absence of direct delivery for single transmembrane apical proteins or their "secretory" forms in polarized hepatic cells
    • Bastaki, M., Braiterman, L. T., Johns, D. C., Chen, Y. H., and Hubbard, A. L. (2002). Absence of direct delivery for single transmembrane apical proteins or their "secretory" forms in polarized hepatic cells. Mol. Biol. Cell 13, 225-237.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 225-237
    • Bastaki, M.1    Braiterman, L.T.2    Johns, D.C.3    Chen, Y.H.4    Hubbard, A.L.5
  • 16
    • 0034617129 scopus 로고    scopus 로고
    • Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors
    • Bilder, D., Li, M., and 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
  • 18
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D. A., and London, E. (2000). Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275, 17221-17224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 19
    • 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, P. S., Wang, E., Aroeti, B., Chapin, S. J., Mostov, K. E., and Dunn, K. W. (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
  • 20
    • 0028267096 scopus 로고
    • Phorbol myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells
    • Cardone, M. H., Smith, B. L., Song, W., Mochly-Rosen, D., and Mostov, K. E. (1994). Phorbol myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells. J. Cell Biol. 124, 717-727.
    • (1994) J. Cell Biol. , vol.124 , pp. 717-727
    • Cardone, M.H.1    Smith, B.L.2    Song, W.3    Mochly-Rosen, D.4    Mostov, K.E.5
  • 21
    • 0033606766 scopus 로고    scopus 로고
    • Sec1p binds to SNARE complexes and concentrates at sites of secretion
    • Carr, C. M., Grote, E., Munson, M., Hughson, F. M., and Novick, P. J. (1999). Sec1p binds to SNARE complexes and concentrates at sites of secretion. J. Cell Biol. 146, 333-344.
    • (1999) J. Cell Biol. , vol.146 , pp. 333-344
    • Carr, C.M.1    Grote, E.2    Munson, M.3    Hughson, F.M.4    Novick, P.J.5
  • 22
    • 0035794533 scopus 로고    scopus 로고
    • GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment
    • Chatterjee, S., Smith, E. R., Hanada, K., Stevens, V. L., and Mayor, S. (2001). GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment. EMBO J. 20, 1583-1592.
    • (2001) EMBO J. , vol.20 , pp. 1583-1592
    • Chatterjee, S.1    Smith, E.R.2    Hanada, K.3    Stevens, V.L.4    Mayor, S.5
  • 23
    • 0036226069 scopus 로고    scopus 로고
    • Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells
    • Chen, Y. H., Lu, Q., Goodenough, D. A., and Jeansonne, B. (2002). Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells. Mol. Biol. Cell 13, 1227-1237.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1227-1237
    • Chen, Y.H.1    Lu, Q.2    Goodenough, D.A.3    Jeansonne, B.4
  • 24
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells
    • Cheong, K. H., Zacchetti, D., Schneeberger, E. E., and Simons, K. (1999). VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc. Natl. Acad. Sci. USA 96, 6241-6248.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6241-6248
    • Cheong, K.H.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 25
    • 0034903162 scopus 로고    scopus 로고
    • Selective control of basolateral membrane protein polarity by cdc42
    • Cohen, D., Müsch, A., and Rodriguez-Boulan, E. (2001). Selective control of basolateral membrane protein polarity by cdc42. Traffic 2, 556-564.
    • (2001) Traffic , vol.2 , pp. 556-564
    • Cohen, D.1    Müsch, A.2    Rodriguez-Boulan, E.3
  • 26
    • 0031958909 scopus 로고    scopus 로고
    • Expression of the cyclin kinase inhibitor, p27kip1, in developing and mature human kidney
    • Combs, H. L., Shankland, S. J., Setzer, S. V., Hudkins, K. L., and Alpers, C. E. (1998). Expression of the cyclin kinase inhibitor, p27kip1, in developing and mature human kidney. Kidney Int. 53, 892-896.
    • (1998) Kidney Int. , vol.53 , pp. 892-896
    • Combs, H.L.1    Shankland, S.J.2    Setzer, S.V.3    Hudkins, K.L.4    Alpers, C.E.5
  • 27
    • 0035121553 scopus 로고    scopus 로고
    • Role of p27(Kip1) in human intestinal cell differentiation
    • Deschenes, C., Vezina, A., Beaulieu, J. F., and Rivard, N. (2001). Role of p27(Kip1) in human intestinal cell differentiation. Gastroenterology 120, 423-438.
    • (2001) Gastroenterology , vol.120 , pp. 423-438
    • Deschenes, C.1    Vezina, A.2    Beaulieu, J.F.3    Rivard, N.4
  • 28
    • 0037166331 scopus 로고    scopus 로고
    • Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins
    • Doray, B., Bruns, K., Ghosh, P., and Kornfeld, S. (2002). Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins. J. Biol. Chem. 277, 18477-18482.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18477-18482
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.4
  • 30
    • 0029995656 scopus 로고    scopus 로고
    • The polymeric immunoglobulin receptor is the major calmodulin-binding protein in an endosome fraction from rat liver enriched in recycling receptors
    • Enrich, C., Jäckle, S., and Havel, R. J. (1996). The polymeric immunoglobulin receptor is the major calmodulin-binding protein in an endosome fraction from rat liver enriched in recycling receptors. Hepatology 24, 226-232.
    • (1996) Hepatology , vol.24 , pp. 226-232
    • Enrich, C.1    Jäckle, S.2    Havel, R.J.3
  • 31
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein
    • Fath, K. R., and Burgess, D. R. (1993). Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein. J. Cell Biol. 120, 117-127.
    • (1993) J. Cell Biol. , vol.120 , pp. 117-127
    • Fath, K.R.1    Burgess, D.R.2
  • 32
    • 0030780090 scopus 로고
    • Molecular motors and a spectrin matrix associate with Golgi membranes in vitro
    • Fath, K. R., Trimbur, G. M., and Burgess, D. R. (1994). Molecular motors and a spectrin matrix associate with Golgi membranes in vitro. J. Cell Biol. 139, 1169-1181.
    • (1994) J. Cell Biol. , vol.139 , pp. 1169-1181
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 33
    • 0028209329 scopus 로고
    • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells
    • Fiedler, K., Parton, R. G., Kellner, R., Etzold, T., and Simons, K. (1994). VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO J. 13, 1729-1740.
    • (1994) EMBO J. , vol.13 , pp. 1729-1740
    • Fiedler, K.1    Parton, R.G.2    Kellner, R.3    Etzold, T.4    Simons, K.5
  • 34
    • 0034990659 scopus 로고    scopus 로고
    • Caveolae and signaling
    • Fielding, C. J. (2001). Caveolae and signaling. Curr. Opin. Lipidol. 12, 281-287.
    • (2001) Curr. Opin. Lipidol. , vol.12 , pp. 281-287
    • Fielding, C.J.1
  • 35
    • 0035937156 scopus 로고    scopus 로고
    • Binding of AP2 to sorting signals is modulated by AP2 phosphorylation
    • Fingerhut, A., von Figura, K., and Höning, S. (2001). Binding of AP2 to sorting signals is modulated by AP2 phosphorylation. J. Biol. Chem. 276, 5476-5482.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5476-5482
    • Fingerhut, A.1    Von Figura, K.2    Höning, S.3
  • 36
    • 85047682087 scopus 로고    scopus 로고
    • Checkpoints for vesicular traffic?
    • Fiset, A., and Faure, R. (2001). Checkpoints for vesicular traffic? Biochem. Cell Biol. 79, 579-585.
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 579-585
    • Fiset, A.1    Faure, R.2
  • 37
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Fölsch, H., Ohno, H., Bonifacino, J. S., and 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
    • Fölsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 38
    • 0035809211 scopus 로고    scopus 로고
    • Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells
    • Fölsch, H., Pypaert, M., Schu, P., and 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
    • Fölsch, H.1    Pypaert, M.2    Schu, P.3    Mellman, I.4
  • 40
    • 0037093470 scopus 로고    scopus 로고
    • Regulation of Cdc42-mediated morphological effects: A novel function for p53
    • Gadea, G., Lapasset, L., Gauthier-Rouviere, C., and Roux, P. (2002). Regulation of Cdc42-mediated morphological effects: A novel function for p53. EMBO J. 21, 2373-2382.
    • (2002) EMBO J. , vol.21 , pp. 2373-2382
    • Gadea, G.1    Lapasset, L.2    Gauthier-Rouviere, C.3    Roux, P.4
  • 41
    • 0033836520 scopus 로고    scopus 로고
    • The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
    • Gagescu, R., Demaurex, N., Parton, R. G., Hunziker, W., Huber, L. A., and Gruenberg, J. (2000). The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Mol. Biol. Cell 11, 2775-2791.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2775-2791
    • Gagescu, R.1    Demaurex, N.2    Parton, R.G.3    Hunziker, W.4    Huber, L.A.5    Gruenberg, J.6
  • 43
    • 0035206785 scopus 로고    scopus 로고
    • Supramaximal cholecystokinin displaces Munc18c from the pancreatic acinar basal surface, redirecting apical exocytosis to the basal membrane
    • Gaisano, H. Y., Lutz, M. P., Leser, J., Sheu, L., Lynch, G., Tang, L., Tamori, Y., Trimble, W. S., and Salapatek, A. M. (2001). Supramaximal cholecystokinin displaces Munc18c from the pancreatic acinar basal surface, redirecting apical exocytosis to the basal membrane. J. Clin. Invest. 108, 1597-1611.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1597-1611
    • Gaisano, H.Y.1    Lutz, M.P.2    Leser, J.3    Sheu, L.4    Lynch, G.5    Tang, L.6    Tamori, Y.7    Trimble, W.S.8    Salapatek, A.M.9
  • 44
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • Galbiati, F., Volonte, D., Engelman, J. A., Watanabe, G., Burk, R., Pestell, R. G., and Lisanti, M. P. (1998). Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. EMBO J. 17, 6633-6648.
    • (1998) EMBO J. , vol.17 , pp. 6633-6648
    • Galbiati, F.1    Volonte, D.2    Engelman, J.A.3    Watanabe, G.4    Burk, R.5    Pestell, R.G.6    Lisanti, M.P.7
  • 45
    • 0035158471 scopus 로고    scopus 로고
    • Caveolin-1 expression negatively regulates cell cycle progression by inducing G(0)/G(1) arrest via a p53/p21(WAF1/Cip1)-dependent mechanism
    • Galbiati, F., Volonte, D., Liu, J., Capozza, F., Frank, P. G., Zhu, L., Pestell, R. G., and Lisanti, M. P. (2001). Caveolin-1 expression negatively regulates cell cycle progression by inducing G(0)/G(1) arrest via a p53/p21(WAF1/Cip1)-dependent mechanism. Mol. Biol. Cell 12, 2229-2244.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2229-2244
    • Galbiati, F.1    Volonte, D.2    Liu, J.3    Capozza, F.4    Frank, P.G.5    Zhu, L.6    Pestell, R.G.7    Lisanti, M.P.8
  • 46
    • 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, V. V., Raposo, G., Tian, J. M., Karin, M., Niemann, H., and 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, 1437-1448.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1437-1448
    • 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
  • 47
    • 0034596012 scopus 로고    scopus 로고
    • Characterization of Cdk2-cyclin E complexes in plasma membrane and endosomes of liver parenchyma. Insulin-dependent regulation
    • Gaulin, J. F., Fiset, A., Fortier, S., and Faure, R. L. (2000). Characterization of Cdk2-cyclin E complexes in plasma membrane and endosomes of liver parenchyma. Insulin-dependent regulation. J. Biol. Chem. 275, 16658-16665.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16658-16665
    • Gaulin, J.F.1    Fiset, A.2    Fortier, S.3    Faure, R.L.4
  • 49
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • Gottardi, C. J., Arpin, M., Fanning, A. S., and Louvard, D. (1996). The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. USA 93, 10779-10784.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 50
    • 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, K. K., Yeaman, C., Anandasabapathy, N., Hsu, S. C., Rodriguez-Boulan, E., Scheller, R. H., and Nelson, W. J. (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    Hsu, S.C.4    Rodriguez-Boulan, E.5    Scheller, R.H.6    Nelson, W.J.7
  • 51
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo, W., Roth, D., Walch-Solimena, C., and Novick, P. (1999). The exocyst is an effector for Sec4p, 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
  • 52
    • 0034709549 scopus 로고    scopus 로고
    • Protein kinase A-dependent phosphorylation of aquaporin-1
    • Han, Z., and Patil, R. V. (2000). Protein kinase A-dependent phosphorylation of aquaporin-1. Biochem. Biophys. Res. Commun. 273, 328-332.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 328-332
    • Han, Z.1    Patil, R.V.2
  • 53
    • 0033044626 scopus 로고    scopus 로고
    • Transcytosis of immunoglobulin A in the mouse enterocyte occurs through glycolipid raft- and rab17-containing compartments
    • Hansen, G. H., Niels-Christiansen, L. L., Immerdal, L., Hunziker, W., Kenny, A. J., and Danielsen, E. M. (1999). Transcytosis of immunoglobulin A in the mouse enterocyte occurs through glycolipid raft- and rab17-containing compartments. Gastroenterology 116, 610-622.
    • (1999) Gastroenterology , vol.116 , pp. 610-622
    • Hansen, G.H.1    Niels-Christiansen, L.L.2    Immerdal, L.3    Hunziker, W.4    Kenny, A.J.5    Danielsen, E.M.6
  • 54
    • 0034685807 scopus 로고    scopus 로고
    • Characterization of rapid membrane internalization and recycling
    • Hao, M., and Maxfield, F. R. (2000). Characterization of rapid membrane internalization and recycling. J. Biol. Chem. 275, 15279-15286.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15279-15286
    • Hao, M.1    Maxfield, F.R.2
  • 55
    • 0032168152 scopus 로고    scopus 로고
    • Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway
    • Heinrich, P. C., Behrmann, I., Müller-Newen, G., Schaper, F., and Graeve, L. (1998). Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway. Biochem. J. 334, 297-314.
    • (1998) Biochem. J. , vol.334 , pp. 297-314
    • Heinrich, P.C.1    Behrmann, I.2    Müller-Newen, G.3    Schaper, F.4    Graeve, L.5
  • 56
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg, K., Miller, C. M., Ellenberg, J., Presley, J. F., Siggia, E. D., Phair, R. D., and Lippincott-Schwartz, J. (1998). Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143, 1485-1503.
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6    Lippincott-Schwartz, J.7
  • 58
    • 0033922431 scopus 로고    scopus 로고
    • Lipid trafficking and sorting: How cholesterol is filling gaps
    • Hoekstra, D., and van IJzendoorn, S. C. D. (2000). Lipid trafficking and sorting: How cholesterol is filling gaps. Curr. Opin. Cell Biol. 12, 496-502.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 496-502
    • Hoekstra, D.1    Van IJzendoorn, S.C.D.2
  • 59
    • 0034789931 scopus 로고    scopus 로고
    • The organizing potential of sphingolipids in intracellular membrane transport
    • Holthuis, J. C., Pomorski, T., Raggers, R. J., Sprong, H., and van Meer, G. (2001). The organizing potential of sphingolipids in intracellular membrane transport. Physiol. Rev. 81, 1689-1723.
    • (2001) Physiol. Rev. , vol.81 , pp. 1689-1723
    • Holthuis, J.C.1    Pomorski, T.2    Raggers, R.J.3    Sprong, H.4    Van Meer, G.5
  • 60
    • 0035424718 scopus 로고    scopus 로고
    • Implications of lipid microdomains for membrane curvature, budding and fission
    • Huttner, W. B., and Zimmerberg, J. (2001). Implications of lipid microdomains for membrane curvature, budding and fission. Curr. Opin. Cell Biol. 13, 478-484.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 478-484
    • Huttner, W.B.1    Zimmerberg, J.2
  • 61
    • 0032177419 scopus 로고    scopus 로고
    • Protein and lipid sorting from the trans-Golgi network to the plasma membrane in polarized cells
    • Ikonen, E., and Simons, K. (1998). Protein and lipid sorting from the trans-Golgi network to the plasma membrane in polarized cells. Semin. Cell Dev. Biol. 9, 503-509.
    • (1998) Semin. Cell Dev. Biol. , vol.9 , pp. 503-509
    • Ikonen, E.1    Simons, K.2
  • 62
    • 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., and 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
  • 63
    • 0030820352 scopus 로고    scopus 로고
    • Myosin II is associated with Golgi membranes: Identification of p200 as nonmuscle myosin II on Golgi-derived vesicles
    • Ikonen, E., de Almeid, J. B., Fath, K. R., Burgess, D. R., Ashman, K., Simons, K., and Stow, J. L. (1997). Myosin II is associated with Golgi membranes: Identification of p200 as nonmuscle myosin II on Golgi-derived vesicles. J. Cell Sci. 110, 2155-2164.
    • (1997) J. Cell Sci. , vol.110 , pp. 2155-2164
    • Ikonen, E.1    De Almeid, J.B.2    Fath, K.R.3    Burgess, D.R.4    Ashman, K.5    Simons, K.6    Stow, J.L.7
  • 64
    • 0033658759 scopus 로고    scopus 로고
    • Retroviral gene transfer of signaling molecules into murine fetal hepatocytes defines distinct roles for the STAT3 and ras pathways during hepatic development
    • Ito, Y., Matsui, T., Kamiya, A., Kinoshita, T., and Miyajima, A. (2000). Retroviral gene transfer of signaling molecules into murine fetal hepatocytes defines distinct roles for the STAT3 and ras pathways during hepatic development. Hepatology 32, 1370-1376.
    • (2000) Hepatology , vol.32 , pp. 1370-1376
    • Ito, Y.1    Matsui, T.2    Kamiya, A.3    Kinoshita, T.4    Miyajima, A.5
  • 65
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • Itoh, M., Furuse, M., Morita, K., Kubota, K., Saitou, M., and Tsukita, S. (1999). Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J. Cell Biol. 147, 1351-1363.
    • (1999) J. Cell Biol. , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 66
    • 0029019737 scopus 로고
    • Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus
    • Jackman, M., Firth, M., and Pines, J. (1995). Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus. EMBO J. 14, 1646-1654.
    • (1995) EMBO J. , vol.14 , pp. 1646-1654
    • Jackman, M.1    Firth, M.2    Pines, J.3
  • 67
    • 0035908953 scopus 로고    scopus 로고
    • Apical membrane proteins are transported in distinct vesicular carriers
    • Jacob, R., and Naim, H. Y. (2001). Apical membrane proteins are transported in distinct vesicular carriers. Curr. Biol. 11, 1444-1450.
    • (2001) Curr. Biol. , vol.11 , pp. 1444-1450
    • Jacob, R.1    Naim, H.Y.2
  • 68
    • 0035203604 scopus 로고    scopus 로고
    • AQP2 is a substrate for endogenous PP2B activity within an inner medullary AKAP-signaling complex
    • Jo, I., Ward, D. T., Baum, M. A., Scott, J. D., Coghlan, V. M., Hammond, T. G., and Harris, H. W. (2001). AQP2 is a substrate for endogenous PP2B activity within an inner medullary AKAP-signaling complex. Am. J. Physiol. 281, F958-F965.
    • (2001) Am. J. Physiol. , vol.281
    • Jo, I.1    Ward, D.T.2    Baum, M.A.3    Scott, J.D.4    Coghlan, V.M.5    Hammond, T.G.6    Harris, H.W.7
  • 70
    • 0030772349 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells
    • Katsura, T., Gustafson, C. E., Ausiello, D. A., and Brown, D. (1997). Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells. Am. J. Physiol. 272, F817-F822.
    • (1997) Am. J. Physiol. , vol.272
    • Katsura, T.1    Gustafson, C.E.2    Ausiello, D.A.3    Brown, D.4
  • 71
    • 0031457805 scopus 로고    scopus 로고
    • Post-Golgi biosynthetic trafficking
    • Keller, P., and Simons, K. (1997). Post-Golgi biosynthetic trafficking. J. Cell Sci. 110, 3001-3009.
    • (1997) J. Cell Sci. , vol.110 , pp. 3001-3009
    • Keller, P.1    Simons, K.2
  • 72
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller, P., and 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
  • 73
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • Keller, P., Toomre, D., Diaz, E., White, J., and 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
  • 74
    • 0034638833 scopus 로고    scopus 로고
    • N-Cadherin extracellular repeat 4 mediates epithelial to mesenchymal transition and increased motility
    • Kim, J. B., Islam, S., Kim, Y. J., Prudoff, R. S., Sass, K. M., Wheelock, M. J., and Johnson, K. R. (2000). N-Cadherin extracellular repeat 4 mediates epithelial to mesenchymal transition and increased motility. J. Cell Biol. 151, 1193-1206.
    • (2000) J. Cell Biol. , vol.151 , pp. 1193-1206
    • Kim, J.B.1    Islam, S.2    Kim, Y.J.3    Prudoff, R.S.4    Sass, K.M.5    Wheelock, M.J.6    Johnson, K.R.7
  • 75
    • 0034717284 scopus 로고    scopus 로고
    • Newly synthesized canalicular ABC transporters are directly targeted from the Golgi to the hepatocyte apical domain in rat liver
    • Kipp, H., and Arias, I. M. (2000). Newly synthesized canalicular ABC transporters are directly targeted from the Golgi to the hepatocyte apical domain in rat liver. J. Biol. Chem. 275, 15917-15925.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15917-15925
    • Kipp, H.1    Arias, I.M.2
  • 76
    • 0035831541 scopus 로고    scopus 로고
    • Transporters on demand: Intrahepatic pools of canalicular ATP binding cassette transporters in rat liver
    • Kipp, H., Pichetshote, N., and Arias, I. M. (2001). Transporters on demand: Intrahepatic pools of canalicular ATP binding cassette transporters in rat liver. J. Biol. Chem. 276, 7218-7224.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7218-7224
    • Kipp, H.1    Pichetshote, N.2    Arias, I.M.3
  • 77
    • 0034721080 scopus 로고    scopus 로고
    • Oncostatin M and interleukin 6 inhibit cell cycle progression by prevention of p27kip1 degradation in HepG2 cells
    • Klausen, P., Pedersen, L., Jurlander, J., and Baumann, H. (2000). Oncostatin M and interleukin 6 inhibit cell cycle progression by prevention of p27kip1 degradation in HepG2 cells. Oncogene 19, 3675-3683.
    • (2000) Oncogene , vol.19 , pp. 3675-3683
    • Klausen, P.1    Pedersen, L.2    Jurlander, J.3    Baumann, H.4
  • 78
    • 0037013148 scopus 로고    scopus 로고
    • Role of phosphatidylinositol (4,5) bisphosphate organization in membrane transport by the Unc104 kinesin motor
    • Klopfenstein, D. R., Tomishige, M., Stuurman, N., and Vale, R. D. (2002). Role of phosphatidylinositol (4,5) bisphosphate organization in membrane transport by the Unc104 kinesin motor. Cell 109, 347-358.
    • (2002) Cell , vol.109 , pp. 347-358
    • Klopfenstein, D.R.1    Tomishige, M.2    Stuurman, N.3    Vale, R.D.4
  • 79
    • 0034921558 scopus 로고    scopus 로고
    • Role and identification of protein kinase A anchoring proteins in vasopressin-mediated aquaporin-2 translocation
    • Klussmann, E., and Rosenthal, W. (2001). Role and identification of protein kinase A anchoring proteins in vasopressin-mediated aquaporin-2 translocation. Kidney Int. 60, 446-449.
    • (2001) Kidney Int. , vol.60 , pp. 446-449
    • Klussmann, E.1    Rosenthal, W.2
  • 80
    • 0029024637 scopus 로고
    • Membrane protein trafficking through the common apical endosome compartment of polarized Caco-2 cells
    • Knight, A., Hughson, E., Hopkins, C. R., and Cutler, D. F. (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
  • 81
    • 0026533469 scopus 로고
    • Sphingolipid transport from the trans-Golgi network to the apical surface in permeabilized MDCK cells
    • Kobayashi, T., Pimplikar, S. W., Parton, R. G., Bhakdi, S., and Simons, K. (1992). Sphingolipid transport from the trans-Golgi network to the apical surface in permeabilized MDCK cells. FEBS Lett. 300, 227-231.
    • (1992) FEBS Lett. , vol.300 , pp. 227-231
    • Kobayashi, T.1    Pimplikar, S.W.2    Parton, R.G.3    Bhakdi, S.4    Simons, K.5
  • 82
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski, R., Hall, A., and 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
  • 83
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • Kuehn, M. J., Herrmann, J. M., and Schekman, R. (1998). COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391, 187-190.
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 84
    • 0028595709 scopus 로고
    • Involvement of microtubule motors in basolateral and apical transport in kidney cells
    • Lafont, F., Burkhardt, J. K., and 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
  • 85
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont, F., Lecat, S., Verkade, P., and 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
  • 86
    • 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., and Simons, K. (1999). Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells. Proc. Natl. Acad. Sci. USA 96, 3734-3738.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3734-3738
    • Lafont, F.1    Verkade, P.2    Galli, T.3    Wimmer, C.4    Louvard, D.5    Simons, K.6
  • 87
    • 0035196362 scopus 로고    scopus 로고
    • Insulin-regulated release from the endosomal recycling compartment is regulated by budding of specialized vesicles
    • Lampson, M. A., Schmoranzer, J., Zeigerer, A., Simon, S. M., and McGraw, T. E. (2001). Insulin-regulated release from the endosomal recycling compartment is regulated by budding of specialized vesicles. Mol. Biol. Cell 12, 3489-3501.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3489-3501
    • Lampson, M.A.1    Schmoranzer, J.2    Zeigerer, A.3    Simon, S.M.4    McGraw, T.E.5
  • 88
    • 0035945347 scopus 로고    scopus 로고
    • Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: A role for ArfGAP1
    • Lanoix, J., Ouwendijk, J., Stark, A., Szafer, E., Cassel, D., Dejgaard, K., Weiss, M., and Nilsson, T. (2001). Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: A role for ArfGAP1. J. Cell Biol. 155, 1199-1212.
    • (2001) J. Cell Biol. , vol.155 , pp. 1199-1212
    • Lanoix, J.1    Ouwendijk, J.2    Stark, A.3    Szafer, E.4    Cassel, D.5    Dejgaard, K.6    Weiss, M.7    Nilsson, T.8
  • 89
  • 90
    • 0030991809 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGN
    • Le Borgne, R., and Hoflack, B. (1997). Mannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGN. J. Cell Biol. 137, 335-345.
    • (1997) J. Cell Biol. , vol.137 , pp. 335-345
    • Le Borgne, R.1    Hoflack, B.2
  • 91
    • 0036099767 scopus 로고    scopus 로고
    • Junctions as organizing centers in epithelial cells? A fly perspective
    • Lecuit, T., and Wieschaus, E. (2002). Junctions as organizing centers in epithelial cells? A fly perspective. Traffic 3, 92-97.
    • (2002) Traffic , vol.3 , pp. 92-97
    • Lecuit, T.1    Wieschaus, E.2
  • 92
    • 0345130002 scopus 로고    scopus 로고
    • Maturation of the axonal plasma membrane requires upregulation of sphingomyelin synthesis and formation of protein-lipid complexes
    • Ledesma, M. D., Brügger, B., Bünning, C., Wieland, F. T., and Dotti, C. G. (1999). Maturation of the axonal plasma membrane requires upregulation of sphingomyelin synthesis and formation of protein-lipid complexes. EMBO J. 18, 1761-1771.
    • (1999) EMBO J. , vol.18 , pp. 1761-1771
    • Ledesma, M.D.1    Brügger, B.2    Bünning, C.3    Wieland, F.T.4    Dotti, C.G.5
  • 93
    • 0027072502 scopus 로고
    • Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation
    • Leyte, A., Barr, F. A., Kehlenbach, R. H., and Huttner, W. B. (1992). Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation. EMBO J. 11, 4795-4804.
    • (1992) EMBO J. , vol.11 , pp. 4795-4804
    • Leyte, A.1    Barr, F.A.2    Kehlenbach, R.H.3    Huttner, W.B.4
  • 94
    • 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., and 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
  • 95
    • 0034176003 scopus 로고    scopus 로고
    • IL-15 is highly expressed in inflammatory bowel disease and regulates local T cell-dependent cytokine production
    • Liu, Z., Geboes, K., Colpaert, S., D'Haens, G. R., Rutgeerts, P., and Ceuppens, J. L. (2000). IL-15 is highly expressed in inflammatory bowel disease and regulates local T cell-dependent cytokine production. J. Immunol. 164, 3608-3615.
    • (2000) J. Immunol. , vol.164 , pp. 3608-3615
    • Liu, Z.1    Geboes, K.2    Colpaert, S.3    D'Haens, G.R.4    Rutgeerts, P.5    Ceuppens, J.L.6
  • 96
    • 0005634007 scopus 로고
    • Apical membrane aminopeptidase appears at site of cell-cell contact in cultured kidney epithelial cells
    • Louvard, D. (1980). Apical membrane aminopeptidase appears at site of cell-cell contact in cultured kidney epithelial cells. Proc. Natl. Acad. Sci. USA 77, 4132-4136.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4132-4136
    • Louvard, D.1
  • 97
    • 0033213258 scopus 로고    scopus 로고
    • The SRC family protein tyrosine kinase p62yes controls polymeric IgA transcytosis in vivo
    • Luton, F., Verges, M., Vaerman, J. P., Sudol, M., and Mostov, K. E. (1999). The SRC family protein tyrosine kinase p62yes controls polymeric IgA transcytosis in vivo. Mol. Cell 4, 627-632.
    • (1999) Mol. Cell , vol.4 , pp. 627-632
    • Luton, F.1    Verges, M.2    Vaerman, J.P.3    Sudol, M.4    Mostov, K.E.5
  • 98
    • 0037414770 scopus 로고    scopus 로고
    • Trans-Golgi networks and subapical compartment of HcpG2 cells display different properties in sorting and exiting of sphinglipids
    • Maier, O., and Hoekstra, D. (2001). Trans-Golgi networks and subapical compartment of HcpG2 cells display different properties in sorting and exiting of sphinglipids. J. Biol. Chem. 278, 164-173.
    • (2001) J. Biol. Chem. , vol.278 , pp. 164-173
    • Maier, O.1    Hoekstra, D.2
  • 99
    • 0039741885 scopus 로고    scopus 로고
    • Membrane domains and polarized trafficking of sphingolipids
    • Maier, O., Aït Slimane, T., and Hoekstra, D. (2001). Membrane domains and polarized trafficking of sphingolipids. Semin. Cell Dev. Biol. 12, 149-161.
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 149-161
    • Maier, O.1    Aït Slimane, T.2    Hoekstra, D.3
  • 100
    • 0036293267 scopus 로고    scopus 로고
    • Fluorescent lipid probes: Some properties and applications (a review)
    • Maier, O., Oberle, V., and Hoekstra, D. (2002). Fluorescent lipid probes: Some properties and applications (a review). Chem. Phys. Lipids 116, 3-18.
    • (2002) Chem. Phys. Lipids , vol.116 , pp. 3-18
    • Maier, O.1    Oberle, V.2    Hoekstra, D.3
  • 101
    • 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., and Alonso, M. A. (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
  • 102
    • 0035966049 scopus 로고    scopus 로고
    • MAL mediates apical transport of secretory proteins in polarized epithelial Madin-Darby canine kidney cells
    • Martin-Belmonte, F., Arvan, P., and Alonso, M. A. (2001). MAL mediates apical transport of secretory proteins in polarized epithelial Madin-Darby canine kidney cells. J. Biol. Chem. 276, 49337-49342.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49337-49342
    • Martin-Belmonte, F.1    Arvan, P.2    Alonso, M.A.3
  • 104
    • 0036500155 scopus 로고    scopus 로고
    • K-Ras mediates cytokine-induced formation of E-cadherin-based adherens junctions during liver development
    • Matsui, T., Kinoshita, T., Morikawa, Y., Tohya, K., Katsuki, M., Ito, Y., Kamiya, A., and Miyajima, A. (2002). K-Ras mediates cytokine-induced formation of E-cadherin-based adherens junctions during liver development. EMBO J. 21, 1021-1030.
    • (2002) EMBO J. , vol.21 , pp. 1021-1030
    • Matsui, T.1    Kinoshita, T.2    Morikawa, Y.3    Tohya, K.4    Katsuki, M.5    Ito, Y.6    Kamiya, A.7    Miyajima, A.8
  • 105
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka, K., Orci, L., Amherdt, M., Bednarek, S. Y., Hamamoto, S., Schekman, R., and Yeung, T. (1998). COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93, 263-275.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5    Schekman, R.6    Yeung, T.7
  • 106
    • 0030022935 scopus 로고    scopus 로고
    • A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Mauxion, F., Le Borgne, R., Munier-Lehmann, H., and Hoflack, B. (1996). A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J. Biol. Chem. 271, 2171-2178.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2171-2178
    • Mauxion, F.1    Le Borgne, R.2    Munier-Lehmann, H.3    Hoflack, B.4
  • 107
    • 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
  • 108
    • 0031770769 scopus 로고    scopus 로고
    • MAL, a novel integral membrane protein of human T lymphocytes, associates with glycosylphosphatidylinositol-anchored proteins and Src-like tyrosine kinases
    • Millan, J., and Alonso, M. A. (1998). MAL, a novel integral membrane protein of human T lymphocytes, associates with glycosylphosphatidylinositol-anchored proteins and Src-like tyrosine kinases. Eur. J. Immunol. 28, 3675-3684.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 3675-3684
    • Millan, J.1    Alonso, M.A.2
  • 109
    • 0037155909 scopus 로고    scopus 로고
    • rab4 regulates transport to the apical plasma membrane in Madin-Darby canine kidney cells
    • Mohrmann, K., Leijendekker, R., Gerez, L., and van der Sluijs, P. (2002). rab4 regulates transport to the apical plasma membrane in Madin-Darby canine kidney cells. J. Biol. Chem. 277, 10474-10481.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10474-10481
    • Mohrmann, K.1    Leijendekker, R.2    Gerez, L.3    Van der Sluijs, P.4
  • 111
    • 0031474609 scopus 로고    scopus 로고
    • Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network
    • Muniz, M., Martin, M. E., Hidalgo, J., and Velasco, A. (1997). Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network. Proc. Natl. Acad. Sci. USA 94, 14461-14466.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14461-14466
    • Muniz, M.1    Martin, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 112
    • 0035947771 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitor p27(Kip1) is required for mouse mammary gland morphogenesis and function
    • Muraoka, R. S., Lenferink, A. E., Simpson, J., Brantley, D. M., Roebuck, L. R., Yakes, F. M., and Arteaga, C. L. (2001). Cyclin-dependent kinase inhibitor p27(Kip1) is required for mouse mammary gland morphogenesis and function. J. Cell Biol. 153, 917-932.
    • (2001) J. Cell Biol. , vol.153 , pp. 917-932
    • Muraoka, R.S.1    Lenferink, A.E.2    Simpson, J.3    Brantley, D.M.4    Roebuck, L.R.5    Yakes, F.M.6    Arteaga, C.L.7
  • 113
    • 0040971539 scopus 로고    scopus 로고
    • Myosin II is involved in the production of constitutive transport vesicles from the TGN
    • Müsch, A., Cohen, D., and Rodriguez-Boulan, E. (1997). Myosin II is involved in the production of constitutive transport vesicles from the TGN. J. Cell Biol. 138, 291-306.
    • (1997) J. Cell Biol. , vol.138 , pp. 291-306
    • Müsch, A.1    Cohen, D.2    Rodriguez-Boulan, E.3
  • 114
    • 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
    • Müsch, A., Cohen, D., Yeaman, C., Nelson, W. J., Rodriguez-Boulan, E., and Brennwald, P. J. (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
    • Müsch, A.1    Cohen, D.2    Yeaman, C.3    Nelson, W.J.4    Rodriguez-Boulan, E.5    Brennwald, P.J.6
  • 115
    • 0028289669 scopus 로고
    • Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells
    • Nathke, I. S., Hinck, L., Swedlow, J. R., Papkoff, J., and Nelson, W. J. (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
  • 116
    • 0028270798 scopus 로고
    • ADP ribosylation factor and a 14-kD polypeptide are associated with heparan sulfate-carrying post-trans-Golgi network secretory vesicles in rat hepatocytes
    • Nickel, W., Huber, L. A., Kahn, R. A., Kipper, N., Barthel, A., Fasshauer, D., and Söling, H. D. (1994). ADP ribosylation factor and a 14-kD polypeptide are associated with heparan sulfate-carrying post-trans-Golgi network secretory vesicles in rat hepatocytes. J. Cell Biol. 125, 721-732.
    • (1994) J. Cell Biol. , vol.125 , pp. 721-732
    • Nickel, W.1    Huber, L.A.2    Kahn, R.A.3    Kipper, N.4    Barthel, A.5    Fasshauer, D.6    Söling, H.D.7
  • 117
    • 0032547843 scopus 로고    scopus 로고
    • Reconstitution of mammary gland development in vitro: Requirement of c-met and c-erbB2 signaling for branching and alveolar morphogenesis
    • Niemann, C., Brinkmann, V., Spitzer, E., Hartmann, G., Sachs, M., Naundorf, H., and Birchmeier, W. (1998). Reconstitution of mammary gland development in vitro: Requirement of c-met and c-erbB2 signaling for branching and alveolar morphogenesis. J. Cell Biol. 143, 533-545.
    • (1998) J. Cell Biol. , vol.143 , pp. 533-545
    • Niemann, C.1    Brinkmann, V.2    Spitzer, E.3    Hartmann, G.4    Sachs, M.5    Naundorf, H.6    Birchmeier, W.7
  • 118
    • 0035929649 scopus 로고    scopus 로고
    • Interleukin-2 receptor beta subunit-dependent and -independent regulation of intestinal epithelial tight junctions
    • Nishiyama, R., Sakaguchi, T., Kinugasa, T., Gu, X., MacDermott, R. P., Podolsky, D. K., and Reinecker, H. C. (2001). Interleukin-2 receptor beta subunit-dependent and -independent regulation of intestinal epithelial tight junctions. J. Biol. Chem. 276, 35571-35580.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35571-35580
    • Nishiyama, R.1    Sakaguchi, T.2    Kinugasa, T.3    Gu, X.4    MacDermott, R.P.5    Podolsky, D.K.6    Reinecker, H.C.7
  • 119
    • 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., and 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
  • 121
    • 0031786378 scopus 로고    scopus 로고
    • An immunologically distinct beta-adaptin on tubulovesicles of gastric oxyntic cells
    • Okamoto, C. T., and Jeng, Y. Y. (1998). An immunologically distinct beta-adaptin on tubulovesicles of gastric oxyntic cells. Am. J. Physiol. 275, C1323-C1329.
    • (1998) Am. J. Physiol. , vol.275
    • Okamoto, C.T.1    Jeng, Y.Y.2
  • 122
    • 0028358382 scopus 로고
    • Rapid internalization of the polymeric immunoglobulin receptor requires phosphorylated serine 726
    • Okamoto, C. T., Song, W., Bomsel, M., and Mostov, K. E. (1994). Rapid internalization of the polymeric immunoglobulin receptor requires phosphorylated serine 726. J. Biol. Chem. 269, 15676-15682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15676-15682
    • Okamoto, C.T.1    Song, W.2    Bomsel, M.3    Mostov, K.E.4
  • 123
    • 0037122726 scopus 로고    scopus 로고
    • Regulation of protein and vesicle trafficking at the apical membrane of epithelial cells
    • Okamoto, C. T., Li, R., Zhang, Z., Jeng, Y. Y., and Chew, C. S. (2002). Regulation of protein and vesicle trafficking at the apical membrane of epithelial cells. J. Control. Release. 78, 35-41.
    • (2002) J. Control. Release , vol.78 , pp. 35-41
    • Okamoto, C.T.1    Li, R.2    Zhang, Z.3    Jeng, Y.Y.4    Chew, C.S.5
  • 124
    • 0033593332 scopus 로고    scopus 로고
    • Interactions of the AP-1 Golgi adaptor with the polymeric immunoglobulin receptor and their possible role in mediating brefeldin A-sensitive basolateral targeting from the trans-Golgi network
    • Orzech, E., Schlessinger, K., Weiss, A., Okamoto, C. T., and Aroeti, B. (1999). Interactions of the AP-1 Golgi adaptor with the polymeric immunoglobulin receptor and their possible role in mediating brefeldin A-sensitive basolateral targeting from the trans-Golgi network. J. Biol. Chem. 274, 2201-2215.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2201-2215
    • Orzech, E.1    Schlessinger, K.2    Weiss, A.3    Okamoto, C.T.4    Aroeti, B.5
  • 125
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer, D. J., Helms, J. B., Beckers, C. J., Orci, L., and Rothman, J. E. (1993). Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J. Biol. Chem. 268, 12083-12089.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12083-12089
    • Palmer, D.J.1    Helms, J.B.2    Beckers, C.J.3    Orci, L.4    Rothman, J.E.5
  • 126
    • 0034442086 scopus 로고    scopus 로고
    • On the mechanism of intracellular membrane fusion: In search of the genuine fusion factor
    • Pecheur, E. I., Maier, O., and Hoekstra, D. (2000). On the mechanism of intracellular membrane fusion: In search of the genuine fusion factor. Biosci. Rep. 20, 613-631.
    • (2000) Biosci. Rep. , vol.20 , pp. 613-631
    • Pecheur, E.I.1    Maier, O.2    Hoekstra, D.3
  • 127
    • 0031305752 scopus 로고    scopus 로고
    • SNAREs and the organization of the secretory pathway
    • Pelham, H. R. (1997). SNAREs and the organization of the secretory pathway. Eur. J. Cell Biol. 74, 311-314.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 311-314
    • Pelham, H.R.1
  • 129
    • 0032387652 scopus 로고    scopus 로고
    • Morphogenetic mechanisms of epithelial tubulogenesis: MDCK cell polarity is transiently rearranged without loss of cell-cell contact during scatter factor/hepatocyte growth factor-induced tubulogenesis
    • Pollack, A. L., Runyan, R. B., and Mostov, K. E. (1998). Morphogenetic mechanisms of epithelial tubulogenesis: MDCK cell polarity is transiently rearranged without loss of cell-cell contact during scatter factor/hepatocyte growth factor-induced tubulogenesis. Dev. Biol. 204, 64-79.
    • (1998) Dev. Biol. , vol.204 , pp. 64-79
    • Pollack, A.L.1    Runyan, R.B.2    Mostov, K.E.3
  • 130
    • 0034502463 scopus 로고    scopus 로고
    • A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes
    • Prekeris, R., Klumperman, J., and Scheller, R. H. (2000). A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes. Mol. Cell 6, 1437-1448.
    • (2000) Mol. Cell , vol.6 , pp. 1437-1448
    • Prekeris, R.1    Klumperman, J.2    Scheller, R.H.3
  • 132
    • 0033543699 scopus 로고    scopus 로고
    • Regulation of cAMP-mediated signal transduction via interaction of caveolins with the catalytic subunit of protein kinase A
    • Razani, B., Rubin, C. S., and Lisanti, M. P. (1999). Regulation of cAMP-mediated signal transduction via interaction of caveolins with the catalytic subunit of protein kinase A. J. Biol. Chem. 274, 26353-26360.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26353-26360
    • Razani, B.1    Rubin, C.S.2    Lisanti, M.P.3
  • 133
    • 0037193471 scopus 로고    scopus 로고
    • ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • Rein, U., Andag, U., Duden, R., Schmitt, H. D., and Spang, A. (2002). ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. J. Cell Biol. 157, 395-404.
    • (2002) J. Cell Biol. , vol.157 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 134
    • 0028101021 scopus 로고
    • Orientation of spindle axis and distribution of plasma membrane proteins during cell division in polarized MDCKII cells
    • Reinsch, S., and Karsenti, E. (1994). Orientation of spindle axis and distribution of plasma membrane proteins during cell division in polarized MDCKII cells. J. Cell Biol. 126, 1509-1526.
    • (1994) J. Cell Biol. , vol.126 , pp. 1509-1526
    • Reinsch, S.1    Karsenti, E.2
  • 135
    • 0034607845 scopus 로고    scopus 로고
    • Munc 18-2, a functional partner of syntaxin 3, controls apical membrane trafficking in epithelial cells
    • Riento, K., Kauppi, M., Keranen, S., and Olkkonen, V. M. (2000). Munc 18-2, a functional partner of syntaxin 3, controls apical membrane trafficking in epithelial cells. J. Biol. Chem. 275, 13476-13483.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13476-13483
    • Riento, K.1    Kauppi, M.2    Keranen, S.3    Olkkonen, V.M.4
  • 136
    • 0035159369 scopus 로고    scopus 로고
    • Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cells
    • Rojas, R., Ruiz, W. G., Leung, S. M., Jou, T. S., and Apodaca, G. (2001). Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 12, 2257-2274.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2257-2274
    • Rojas, R.1    Ruiz, W.G.2    Leung, S.M.3    Jou, T.S.4    Apodaca, G.5
  • 137
    • 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., and Huttner, W. B. (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
  • 138
    • 0030020733 scopus 로고    scopus 로고
    • The protein machinery of vesicle budding and fusion
    • Rothman, J. E. (1996). The protein machinery of vesicle budding and fusion. Protein Sci. 5, 185-194.
    • (1996) Protein Sci. , vol.5 , pp. 185-194
    • Rothman, J.E.1
  • 139
    • 0034305747 scopus 로고    scopus 로고
    • Detergent insoluble microdomains are not involved in transcytosis of polymeric Ig receptor in FRT and MDCK cells
    • Sarnataro, D., Nitsch, L., Hunziker, W., and Zurzolo, C. (2000). Detergent insoluble microdomains are not involved in transcytosis of polymeric Ig receptor in FRT and MDCK cells. Traffic 1, 794-802.
    • (2000) Traffic , vol.1 , pp. 794-802
    • Sarnataro, D.1    Nitsch, L.2    Hunziker, W.3    Zurzolo, C.4
  • 140
    • 0028270799 scopus 로고
    • Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers
    • Saucan, L., and Palade, G. E. (1994). Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers. J. Cell Biol. 125, 733-741.
    • (1994) J. Cell Biol. , vol.125 , pp. 733-741
    • Saucan, L.1    Palade, G.E.2
  • 141
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Schiffele, P., Peranen, J., and Simons, K. (1995). N-glycans as apical sorting signals in epithelial cells. Nature 78, 96-98.
    • (1995) Nature , vol.78 , pp. 96-98
    • Schiffele, P.1    Peranen, J.2    Simons, K.3
  • 143
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S. L. (1997). Clathrin-coated vesicle formation and protein sorting: An integrated process. Annu. Rev. Biochem. 66, 511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 144
    • 0036156444 scopus 로고    scopus 로고
    • Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes
    • Sheff, D. R., Kroschewski, R., and 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
  • 145
    • 0036167130 scopus 로고    scopus 로고
    • AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells
    • Simmen, T., Höning, S., Icking, A., Tikkanen, R., and 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    Höning, S.2    Icking, A.3    Tikkanen, R.4    Hunziker, W.5
  • 146
    • 0029911415 scopus 로고    scopus 로고
    • The production of post-Golgi vesicles requires a protein kinase C-like molecule, but not its phosphorylating activity
    • Simon, J. P., Ivanov, I. E., Adesnik, M., and Sabatini, D. D. (1996). The production of post-Golgi vesicles requires a protein kinase C-like molecule, but not its phosphorylating activity. J. Cell Biol. 135, 355-370.
    • (1996) J. Cell Biol. , vol.135 , pp. 355-370
    • Simon, J.P.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 147
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and 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
  • 148
    • 0030890718 scopus 로고    scopus 로고
    • Gp130 and the interleukin-6 family of cytokines
    • Taga, T., and Kishimoto, T. (1997). Gp130 and the interleukin-6 family of cytokines. Annu. Rev. Immunol. 15, 797-819.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 797-819
    • Taga, T.1    Kishimoto, T.2
  • 149
    • 0035958856 scopus 로고    scopus 로고
    • Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains
    • Takatsu, H., Katoh, Y., Shiba, Y., and Nakayama, K. (2001). Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276, 28541-28545.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28541-28545
    • Takatsu, H.1    Katoh, Y.2    Shiba, Y.3    Nakayama, K.4
  • 150
    • 0037101770 scopus 로고    scopus 로고
    • GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors
    • Takatsu, H., Yoshino, K., Toda, K., and Nakayama, K. (2002). GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors. Biochem. J. 365, 369-378.
    • (2002) Biochem. J. , vol.365 , pp. 369-378
    • Takatsu, H.1    Yoshino, K.2    Toda, K.3    Nakayama, K.4
  • 151
    • 0030969764 scopus 로고    scopus 로고
    • Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4
    • Tellam, J. T., Macaulay, S. L., McIntosh, S., Hewish, D. R., Ward, C. W., and James, D. E. (1997). Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4. J. Biol. Chem. 272, 6179-6186.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6179-6186
    • Tellam, J.T.1    Macaulay, S.L.2    McIntosh, S.3    Hewish, D.R.4    Ward, C.W.5    James, D.E.6
  • 152
    • 0033049383 scopus 로고    scopus 로고
    • Dissociation between growth arrest and differentiation in Caco-2 subclone expressing high levels of sucrase
    • Tian, J. Q., and Quaroni, A. (1999a). Dissociation between growth arrest and differentiation in Caco-2 subclone expressing high levels of sucrase. Am. J. Physiol. 276, G1094-G1104.
    • (1999) Am. J. Physiol. , vol.276
    • Tian, J.Q.1    Quaroni, A.2
  • 153
    • 0033027864 scopus 로고    scopus 로고
    • Involvement of p21(WAF1/Cip1) and p27(Kip1) in intestinal epithelial cell differentiation
    • Tian, J. Q., and Quaroni, A. (1999b). Involvement of p21(WAF1/Cip1) and p27(Kip1) in intestinal epithelial cell differentiation. Am. J. Physiol. 276, C1245-C1258.
    • (1999) Am. J. Physiol. , vol.276
    • Tian, J.Q.1    Quaroni, A.2
  • 154
    • 0030816038 scopus 로고    scopus 로고
    • The trans-Golgi network: A late secretory sorting station
    • Traub, L. M., and Kornfeld, S. (1997). The trans-Golgi network: A late secretory sorting station. Curr. Opin. Cell Biol. 9, 527-533.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 527-533
    • Traub, L.M.1    Kornfeld, S.2
  • 155
    • 0035071207 scopus 로고    scopus 로고
    • Mutant cadherin affects epithelial morphogenesis and invasion, but not transformation
    • Troxell, M. L., Loftus, D. J., Nelson, W. J., and Marrs, J. A. (2001). Mutant cadherin affects epithelial morphogenesis and invasion, but not transformation. J. Cell Sci. 114, 1237-1246.
    • (2001) J. Cell Sci. , vol.114 , pp. 1237-1246
    • Troxell, M.L.1    Loftus, D.J.2    Nelson, W.J.3    Marrs, J.A.4
  • 157
    • 0026446550 scopus 로고
    • Reversible phosphorylation-dephosphorylation determines the localization of rab4 during the cell cycle
    • van der Sluijs, P., Hull, M., Huber, L. A., Male, P., Goud, B., and Mellman, I. (1992). Reversible phosphorylation-dephosphorylation determines the localization of rab4 during the cell cycle. EMBO J. 11, 4379-4389.
    • (1992) EMBO J. , vol.11 , pp. 4379-4389
    • Van der Sluijs, P.1    Hull, M.2    Huber, L.A.3    Male, P.4    Goud, B.5    Mellman, I.6
  • 158
    • 0037011151 scopus 로고    scopus 로고
    • Oncostatin M regulates membrane traffic and stimulates bile canalicular membrane biogenesis in HepG2 cells
    • van der Wouden, J. M., van IJendoorn, J. C. D., and Hoekstra, D. (2002). Oncostatin M regulates membrane traffic and stimulates bile canalicular membrane biogenesis in HepG2 cells. EMBO J. 21, 6409-6418.
    • (2002) EMBO J. , vol.21 , pp. 6409-6418
    • Van der Wouden, J.M.1    Van IJendoorn, J.C.D.2    Hoekstra, D.3
  • 159
    • 0028786817 scopus 로고
    • Differential targeting of glucosylceramide and galactosylceramide analogues after synthesis but not during transcytosis in Madin-Darby canine kidney cells
    • van Genderen, I., and van Meer, G. (1995). Differential targeting of glucosylceramide and galactosylceramide analogues after synthesis but not during transcytosis in Madin-Darby canine kidney cells. J. Cell Biol. 131, 645-654.
    • (1995) J. Cell Biol. , vol.131 , pp. 645-654
    • Van Genderen, I.1    Van Meer, G.2
  • 160
    • 0031852648 scopus 로고    scopus 로고
    • (Glyco)sphingolipids are sorted in sub-apical compartments in HepG2 cells: A role for non-Golgi-related intracellular sites in the polarized distribution of (glyco)sphingolipids
    • van IJzendoorn, S. C. D., and Hoekstra, D. (1998). (Glyco)sphingolipids are sorted in sub-apical compartments in HepG2 cells: A role for non-Golgi-related intracellular sites in the polarized distribution of (glyco)sphingolipids. J. Cell Biol. 142, 683-696.
    • (1998) J. Cell Biol. , vol.142 , pp. 683-696
    • Van IJzendoorn, S.C.D.1    Hoekstra, D.2
  • 161
    • 0032830851 scopus 로고    scopus 로고
    • Polarized sphingolipid transport from the subapical compartment: Evidence for distinct sphingolipid domains
    • van IJzendoorn, S. C. D., and Hoekstra, D. (1999). Polarized sphingolipid transport from the subapical compartment: Evidence for distinct sphingolipid domains. Mol. Biol. Cell 10, 3449-3461.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3449-3461
    • Van IJzendoorn, S.C.D.1    Hoekstra, D.2
  • 162
    • 0034016431 scopus 로고    scopus 로고
    • Polarized sphingolipid transport from the subapical compartment changes during cell polarity development
    • van IJzendoorn, S. C. D., and Hoekstra, D. (2000). Polarized sphingolipid transport from the subapical compartment changes during cell polarity development. Mol. Biol. Cell 11, 1093-1101.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1093-1101
    • Van IJzendoorn, S.C.D.1    Hoekstra, D.2
  • 164
    • 0036480017 scopus 로고    scopus 로고
    • Direct interaction between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells
    • van IJzendoorn, S. C. D., Tuvim, M. J., Weimbs, T., Dickey, B. F., and Mostov, K. E. (2002). Direct interaction between Rab3b 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
  • 165
    • 0023432865 scopus 로고
    • Sorting of sphingolipids in epithelial (Madin-Darby canine kidney) cells
    • van Meer, G., Stelzer, E. H., Wijnaendts-van-Resandt, R. W., and Simons, K. (1987). Sorting of sphingolipids in epithelial (Madin-Darby canine kidney) cells. J. Cell Biol. 105, 1623-1635.
    • (1987) J. Cell Biol. , vol.105 , pp. 1623-1635
    • Van Meer, G.1    Stelzer, E.H.2    Wijnaendts-van-Resandt, R.W.3    Simons, K.4
  • 166
    • 0035823549 scopus 로고    scopus 로고
    • Protein kinase A regulates expression of p27(kip1) and cyclin D3 to suppress proliferation of leukemic T cell lines
    • van Oirschot, B. A., Stahl, M., Lens, S. M., and Medema, R. H. (2001). Protein kinase A regulates expression of p27(kip1) and cyclin D3 to suppress proliferation of leukemic T cell lines. J. Biol. Chem. 276, 33854-33860.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33854-33860
    • Van Oirschot, B.A.1    Stahl, M.2    Lens, S.M.3    Medema, R.H.4
  • 167
    • 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, D. E., Salas, P. J., Gundersen, D., and Rodriguez-Boulan, E. (1987). 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
  • 168
    • 0031550224 scopus 로고    scopus 로고
    • Cyclin A is present in the endocytic compartment of rat liver cells and increases during liver regeneration
    • Vergés, M., Castro, A., Jaumot, M., Bachs, O., and Enrich, C. (1997). Cyclin A is present in the endocytic compartment of rat liver cells and increases during liver regeneration. Biochem. Biophys. Res. Commun. 230, 49-53.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 49-53
    • Vergés, M.1    Castro, A.2    Jaumot, M.3    Bachs, O.4    Enrich, C.5
  • 169
    • 0033621149 scopus 로고    scopus 로고
    • A tubular endosomal fraction from rat liver: Biochemical evidence of receptor sorting by default
    • Vergés, M., Havel, R. J., and Mostov, K. E. (1999). A tubular endosomal fraction from rat liver: Biochemical evidence of receptor sorting by default. Proc. Natl. AcadSci. USA 96, 10146-10151.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10146-10151
    • Vergés, M.1    Havel, R.J.2    Mostov, K.E.3
  • 170
    • 0031229420 scopus 로고    scopus 로고
    • Lipid microdomains and membrane trafficking in mammalian cells
    • Verkade, P., and Simons, K. (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
  • 171
    • 0034823910 scopus 로고    scopus 로고
    • Rho kinase regulates tight junction function and is necessary for tight junction assembly in polarized intestinal epithelia
    • Walsh, S. V., Hopkins, A. M., Chen, J., Narumiya, S., Parkos, C. A., and Nusrat, A. (2001). Rho kinase regulates tight junction function and is necessary for tight junction assembly in polarized intestinal epithelia. Gastroenterology. 121, 566-579.
    • (2001) Gastroenterology , vol.121 , pp. 566-579
    • Walsh, S.V.1    Hopkins, A.M.2    Chen, J.3    Narumiya, S.4    Parkos, C.A.5    Nusrat, A.6
  • 172
    • 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, M. K., Antony, C., and 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
  • 173
    • 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, P. S., Aroeti, B., Chapin, S. J., Mostov, K. E., and Dunn, K. W. (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
  • 174
    • 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, J. G., Goldenring, J. R., Hunziker, W., and Dunn, K. W. (2001). Brefeldin A rapidly disrupts plasma membrane polarity by blocking polar sorting in common endosomes of MDCK cells. J. Cell Sci. 114, 3309-3321.
    • (2001) 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
  • 175
    • 0034666356 scopus 로고    scopus 로고
    • Regulation of vesicle trafficking in Madin-Darby canine kidney cells by Rab11a and Rab25
    • Wang, X., Kumar, R., Navarre, J., Casanova, J. E., and Goldenring, J. R. (2000). Regulation of vesicle trafficking in Madin-Darby canine kidney cells by Rab11a and Rab25. 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
  • 176
    • 0030881255 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment
    • West, M. A., Bright, N. A., and Robinson, M. S. (1997). The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment. J. Cell Biol. 138, 1239-1254.
    • (1997) J. Cell Biol. , vol.138 , pp. 1239-1254
    • West, M.A.1    Bright, N.A.2    Robinson, M.S.3
  • 177
    • 0029854499 scopus 로고    scopus 로고
    • Protein kinase C bound to the Golgi apparatus supports the formation of constitutive transport vesicles
    • Westermann, P., Knoblich, M., Maier, O., Lindschau, C., and Haller, H. (1996). Protein kinase C bound to the Golgi apparatus supports the formation of constitutive transport vesicles. Biochem. J. 320, 651-658.
    • (1996) Biochem. J. , vol.320 , pp. 651-658
    • Westermann, P.1    Knoblich, M.2    Maier, O.3    Lindschau, C.4    Haller, H.5
  • 178
    • 0031425958 scopus 로고    scopus 로고
    • Phosphorylation of occludin correlates with occludin localization and function at the tight junction
    • Wong, V. (1997). Phosphorylation of occludin correlates with occludin localization and function at the tight junction. Am. J. Physiol. 273, C1859-C1867.
    • (1997) Am. J. Physiol. , vol.273
    • Wong, V.1
  • 180
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori, T., Keller, P., Roth, M. G., and Simons, K. (1996). Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 133, 247-256.
    • (1996) J. Cell Biol. , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4
  • 182
    • 0034722381 scopus 로고    scopus 로고
    • Tight junction, a platform for trafficking and signaling protein complexes
    • Zahraoui, A., Louvard, D., and Galli, T. (2000). Tight junction, a platform for trafficking and signaling protein complexes. J. Cell Biol. 151, F31-36.
    • (2000) J. Cell Biol. , vol.151
    • Zahraoui, A.1    Louvard, D.2    Galli, T.3
  • 183
    • 0030845928 scopus 로고    scopus 로고
    • Sphingolipid transport to the apical plasma membrane domain in human hepatoma cells is controlled by PKC and PKA activity: A correlation with cell polarity in HepG2 cells
    • Zegers, M. M., and Hoekstra, D. (1997). Sphingolipid transport to the apical plasma membrane domain in human hepatoma cells is controlled by PKC and PKA activity: A correlation with cell polarity in HepG2 cells. J. Cell Biol. 138, 307-321.
    • (1997) J. Cell Biol. , vol.138 , pp. 307-321
    • Zegers, M.M.1    Hoekstra, D.2
  • 184
    • 0032385839 scopus 로고    scopus 로고
    • Mechanisms and functional features of polarized membrane traffic in epithelial and hepatic cells
    • Zegers, M. M., and Hoekstra, D. (1998). Mechanisms and functional features of polarized membrane traffic in epithelial and hepatic cells. Biochem. J. 336, 257-269.
    • (1998) Biochem. J. , vol.336 , pp. 257-269
    • Zegers, M.M.1    Hoekstra, D.2
  • 186
    • 0033609083 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 dependent clathrin-coat assembly on synthetic liposomes
    • Zhu, Y., Drake, M. T., and Kornfeld, S. (1999). ADP-ribosylation factor 1 dependent clathrin-coat assembly on synthetic liposomes. Proc. Natl. Acad. Sci. USA 96, 5013-5018.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5013-5018
    • Zhu, Y.1    Drake, M.T.2    Kornfeld, S.3


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