메뉴 건너뛰기




Volumn 141, Issue 3, 1998, Pages 611-623

In polarized MDCK cells basolateral vesicles arise from clathrin-γ- adaptin-coated domains on endosomal tubules

Author keywords

[No Author keywords available]

Indexed keywords

BREFELDIN A; CLATHRIN; GAMMA ADAPTIN; IMMUNOGLOBULIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 0032482226     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.3.611     Document Type: Article
Times cited : (195)

References (65)
  • 1
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • Aniento, F., F. Gu, R.G. Parton, and J. Gruenberg. 1996. An endosomal COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes. J. Cell Biol. 133:29-42.
    • (1996) J. Cell Biol. , vol.133 , pp. 29-42
    • Aniento, F.1    Gu, F.2    Parton, R.G.3    Gruenberg, J.4
  • 2
    • 0028346520 scopus 로고
    • Receptor mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca, G., L.A. Katz, and K.E. Mostov. 1994. Receptor mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J. Cell Biol. 125: 67-86.
    • (1994) J. Cell Biol. , vol.125 , pp. 67-86
    • Apodaca, G.1    Katz, L.A.2    Mostov, K.E.3
  • 3
    • 0030222342 scopus 로고    scopus 로고
    • Principles of selective transport: Coat complexes hold the key
    • Aridor, M., and W.E. Balch. 1996. Principles of selective transport: coat complexes hold the key. Trends Cell Biol. 6:315-320.
    • (1996) Trends Cell Biol. , vol.6 , pp. 315-320
    • Aridor, M.1    Balch, W.E.2
  • 4
    • 0028342843 scopus 로고
    • Polarized sorting of the polymeric immunoglobulin receptor in the exocytotic and endocytotic pathways is controlled by the same amino acids
    • Aroeti, B., and K.E. Mostov. 1994. Polarized sorting of the polymeric immunoglobulin receptor in the exocytotic and endocytotic pathways is controlled by the same amino acids. EMBO (Eur. Mol. Biol. Organ.) J. 13:2297-2304.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2297-2304
    • Aroeti, B.1    Mostov, K.E.2
  • 5
    • 0028009419 scopus 로고
    • Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome
    • Barroso, M., and E.S. Sztul. 1994. Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome. J. Cell Biol. 124:83-100.
    • (1994) J. Cell Biol. , vol.124 , pp. 83-100
    • Barroso, M.1    Sztul, E.S.2
  • 6
    • 0027421873 scopus 로고
    • A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor
    • Bates, P., J.A.T. Young, and H.E. Varmus. 1993. A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor. Cell. 74:1043-1051.
    • (1993) Cell , vol.74 , pp. 1043-1051
    • Bates, P.1    Young, J.A.T.2    Varmus, H.E.3
  • 7
    • 0027207340 scopus 로고
    • Adaptor selfaggregation, adaptor-receptor recognition and binding of the a-subunit to the plasma membrane contribute to recruitment of adaptor (AP2) components of clathrin-coated pits
    • Chang, M.P., W.G. Mallet, K.E. Mostov, and P.M. Brodsky. 1993. Adaptor selfaggregation, adaptor-receptor recognition and binding of the a-subunit to the plasma membrane contribute to recruitment of adaptor (AP2) components of clathrin-coated pits. EMBO (Eur. Mol. Biol. Organ.) J. 12:2169-2180.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2169-2180
    • Chang, M.P.1    Mallet, W.G.2    Mostov, K.E.3    Brodsky, P.M.4
  • 8
    • 0027997875 scopus 로고
    • Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase
    • Connolly, C., C.E. Futter, C.R. Hopkins, and D.F. Cutler. 1994. Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase. J. Cell Biol. 127:641-652.
    • (1994) J. Cell Biol. , vol.127 , pp. 641-652
    • Connolly, C.1    Futter, C.E.2    Hopkins, C.R.3    Cutler, D.F.4
  • 9
    • 0027536798 scopus 로고
    • The internalisation signal and the phosphorylation site of transferrin receptor are distinct from the main basolateral sorting information
    • Dargemont, C, A. LeBivic, S. Rothenburger, B. Iacopetta, and L. Kuhn. 1993. The internalisation signal and the phosphorylation site of transferrin receptor are distinct from the main basolateral sorting information. EMBO (Eur. Mol. Biol. Organ.) J. 12:1713-1721.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 1713-1721
    • Dargemont, C.1    LeBivic, A.2    Rothenburger, S.3    Iacopetta, B.4    Kuhn, L.5
  • 10
    • 0025674154 scopus 로고
    • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
    • Donaldson, J.G., J. Lippincott-Schwartz, G.S. Bloom, T.E. Kreis, and R.D. Klausner. 1990. Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J. Cell Biol. 111: 2295-2306.
    • (1990) J. Cell Biol. , vol.111 , pp. 2295-2306
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Bloom, G.S.3    Kreis, T.E.4    Klausner, R.D.5
  • 11
    • 0031425955 scopus 로고    scopus 로고
    • Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component ∈-COP
    • Daro, E., D. Sheff, M. Gomez, T. Kreis, and I. Mellman, 1997. Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component ∈-COP. J. Cell Biol. 139:1747-1759.
    • (1997) J. Cell Biol. , vol.139 , pp. 1747-1759
    • Daro, E.1    Sheff, D.2    Gomez, M.3    Kreis, T.4    Mellman, I.5
  • 12
    • 0028969528 scopus 로고
    • Newly synthesised transferrin receptors can be detected in the endosome before they appear on the cell surface
    • Futter, C.E., C.N. Connolly, D.F. Cutler, and C.R. Hopkins. 1995. Newly synthesised 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
  • 13
    • 0029979181 scopus 로고    scopus 로고
    • Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes
    • Futter, C.E., A. Pearse, L. Hewlett, and C.R. Hopkins. 1996. Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes. J. Cell Biol. 132:1011-1023.
    • (1996) J. Cell Biol. , vol.132 , pp. 1011-1023
    • Futter, C.E.1    Pearse, A.2    Hewlett, L.3    Hopkins, C.R.4
  • 14
    • 0026528446 scopus 로고
    • Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to the Golgi apparatus at equal rates in PC-12 cells
    • Green, S.A., and R.B. Kelly. 1992. Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to the Golgi apparatus at equal rates in PC-12 cells. J. Cell Biol. 117: 47-55.
    • (1992) J. Cell Biol. , vol.117 , pp. 47-55
    • Green, S.A.1    Kelly, R.B.2
  • 15
    • 0030812588 scopus 로고    scopus 로고
    • Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes
    • Gu, F., F. Aniento, R. Parton, and J. Gruenberg. 1997. Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes. J. Cell Biol. 139:1183-1195.
    • (1997) J. Cell Biol. , vol.139 , pp. 1183-1195
    • Gu, F.1    Aniento, F.2    Parton, R.3    Gruenberg, J.4
  • 16
    • 0028264318 scopus 로고
    • Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by ∈-COP
    • Guo, Q., E. Vasile, and M. Krieger. 1994. Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by ∈-COP. J. Cell Biol. 125:1213-1224.
    • (1994) J. Cell Biol. , vol.125 , pp. 1213-1224
    • Guo, Q.1    Vasile, E.2    Krieger, M.3
  • 18
    • 0029893859 scopus 로고    scopus 로고
    • The transcytotic pathway of an apical membrane protein (B10) in hepatocytes is similar to that of IgA and occurs via a tubular pericentriolar compartment
    • Hemery, I. A.-M. Durand-Schneider, G. Feldmann, J.-P. Vaerman, and M. Maurice. 1996. The transcytotic pathway of an apical membrane protein (B10) in hepatocytes is similar to that of IgA and occurs via a tubular pericentriolar compartment. J. Cell Sci. 109:1215-1227.
    • (1996) J. Cell Sci. , vol.109 , pp. 1215-1227
    • Hemery, I.1    Durand-Schneider, A.-M.2    Feldmann, G.3    Vaerman, J.-P.4    Maurice, M.5
  • 19
    • 0028169450 scopus 로고
    • Isolation of three classes of conditional lethal Chinese hamster ovary cell mutants with temperature-dependent defects in low density lipoprotein receptor stability and intracellular membrane transport
    • Hobbie, L., A.S. Fisher, S. Lee, A. Flint, and M. Krieger. 1994. Isolation of three classes of conditional lethal Chinese hamster ovary cell mutants with temperature-dependent defects in low density lipoprotein receptor stability and intracellular membrane transport. J. Biol. Chem. 269:20958-20970.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20958-20970
    • Hobbie, L.1    Fisher, A.S.2    Lee, S.3    Flint, A.4    Krieger, M.5
  • 20
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi network: Involvement of a cytoplasmic tyrosine-containing sequence
    • Humphrey, J.S., P.J. Peters, L.C. Yuan, and J.S. Bonafacino. 1993. Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequence. J. Cell Biol. 120:1123-1135.
    • (1993) J. Cell Biol. , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Bonafacino, J.S.4
  • 21
    • 0026091737 scopus 로고
    • Selective inhibition of transcytosis by brefeldin A in MDCK cells
    • Hunziker, W., J.A. Whitney, and I. Mellman. 1991. Selective inhibition of transcytosis by brefeldin A in MDCK cells. Cell. 67:617-628.
    • (1991) Cell , vol.67 , pp. 617-628
    • Hunziker, W.1    Whitney, J.A.2    Mellman, I.3
  • 22
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., M. Tagaya, O. Ullrich, C. Montecucco, and K. Simons. 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
  • 23
    • 0025014580 scopus 로고
    • Role of the human transferrin receptor cytoplasmic domain in endocytosis: Localization of a specific signal sequence for internalization
    • Jing, S., T. Spencer, K. Miller, C. Hopkins, and I.S. Trowbridge. 1990. Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization. J. Cell Biol. 110:283-294.
    • (1990) J. Cell Biol. , vol.110 , pp. 283-294
    • Jing, S.1    Spencer, T.2    Miller, K.3    Hopkins, C.4    Trowbridge, I.S.5
  • 24
    • 0028068272 scopus 로고
    • Coat proteins in intracellular membrane transport
    • Kreis, T.E., and R. Pepperkok. 1994. Coat proteins in intracellular membrane transport. Curr. Opin. Cell Biol. 6:533-537.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 533-537
    • Kreis, T.E.1    Pepperkok, R.2
  • 25
    • 0030053198 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors and ADP-ribosylation factors cooperate for high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Le Borgne, R., G. Griffiths, and B. Hoflack. 1996. Mannose 6-phosphate receptors and ADP-ribosylation factors cooperate for high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J. Biol. Chem. 271:2162-2170.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2162-2170
    • Le Borgne, R.1    Griffiths, G.2    Hoflack, B.3
  • 26
    • 0028871658 scopus 로고
    • Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes
    • Leitinger, B., A. Hille-Rehfeld, and M. Spiess. 1995. Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes. Proc. Natl. Acad. Sci. USA. 92:10109-10113.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10109-10113
    • Leitinger, B.1    Hille-Rehfeld, A.2    Spiess, M.3
  • 27
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., J.G. Donaldson, A. Schweizer, E.G. Berger, H.P. Hauri, L.C. Yuan, and R.D. Klausner. 1990. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell. 60:821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 28
    • 0025940101 scopus 로고
    • Brefeldin A's effects on endosomes, lysosomes and the trans Golgi network suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., L. Yuan, C. Tipper, M. Amherdt, L. Orci, and R.D. Klausner. 1991. Brefeldin A's effects on endosomes, lysosomes and the trans Golgi network suggest a general mechanism for regulating organelle structure and membrane traffic. Cell. 67:601-616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.D.6
  • 29
    • 0029847075 scopus 로고    scopus 로고
    • Differential localisation of syntaxin isoforms in polarized Madin-Darby canine kidney cells
    • Low, S.-H., S.J. Chapin, T. Weimbs, L.G. Komuves, M.K. Bennett, and K.E. Mostov. 1996. Differential localisation of syntaxin isoforms in polarized Madin-Darby canine kidney cells. Mol. Biol. Cell. 7:2007-2018.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2007-2018
    • Low, S.-H.1    Chapin, S.J.2    Weimbs, T.3    Komuves, L.G.4    Bennett, M.K.5    Mostov, K.E.6
  • 30
    • 0026318365 scopus 로고
    • Distribution of newly synthesised lysosomal enzymes on the endocytic pathway of normal rat kidney cells
    • Ludwig, T., G. Griffiths, and B. Hoflack. 1991. Distribution of newly synthesised lysosomal enzymes on the endocytic pathway of normal rat kidney cells. J. Cell Biol. 115:1561-1572.
    • (1991) J. Cell Biol. , vol.115 , pp. 1561-1572
    • Ludwig, T.1    Griffiths, G.2    Hoflack, B.3
  • 31
    • 0027444967 scopus 로고
    • Common signals control low density lipoprotein receptor sorting in endosomes and the Golgi complex of MDCK cells
    • Matter, K., J.A. Whitney, E.M. Yamamoto, and I. Mellman. 1993. Common signals control low density lipoprotein receptor sorting in endosomes and the Golgi complex of MDCK cells. Cell. 74:1053-1064.
    • (1993) Cell , vol.74 , pp. 1053-1064
    • Matter, K.1    Whitney, J.A.2    Yamamoto, E.M.3    Mellman, I.4
  • 32
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., and I. Mellman. 1994. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6:545-554.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 33
    • 0025823445 scopus 로고
    • Transferrin receptors promote the formation of clathrin lattices
    • Miller, K., M. Shipman, I.S. Trowbridge, and C R. Hopkins. 1991. Transferrin receptors promote the formation of clathrin lattices. Cell. 65:621-632.
    • (1991) Cell , vol.65 , pp. 621-632
    • Miller, K.1    Shipman, M.2    Trowbridge, I.S.3    Hopkins, C.R.4
  • 34
    • 0026531638 scopus 로고
    • Plasma membrane protein sorting in polarized epithelial cells
    • Mostov, K.E., G. Apodaca, B. Aroeti, and C. Okamoto. 1992. Plasma membrane protein sorting in polarized epithelial cells. J. Cell Biol. 116:577-583.
    • (1992) J. Cell Biol. , vol.116 , pp. 577-583
    • Mostov, K.E.1    Apodaca, G.2    Aroeti, B.3    Okamoto, C.4
  • 35
    • 0028709374 scopus 로고
    • Recombinant Rous sarcoma virus vectors for avian cells
    • Odorizzi, G., and I.S. Trowbridge. 1994. Recombinant Rous sarcoma virus vectors for avian cells. Methods Cell Biol. 43:79-98.
    • (1994) Methods Cell Biol. , vol.43 , pp. 79-98
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 36
    • 0030905888 scopus 로고    scopus 로고
    • Structural requirements for basolateral sorting on the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells
    • Odorizzi, G., and I.S. Trowbridge. 1997. Structural requirements for basolateral sorting on the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells. J. Cell Biol. 137:1255-1264.
    • (1997) J. Cell Biol. , vol.137 , pp. 1255-1264
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 37
    • 0029820888 scopus 로고    scopus 로고
    • Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism
    • Odorizzi, G., I.S. Trowbridge, and C.R. Hopkins. 1996. Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism. J. Cell Biol. 135:139-152.
    • (1996) J. Cell Biol. , vol.135 , pp. 139-152
    • Odorizzi, G.1    Trowbridge, I.S.2    Hopkins, C.R.3
  • 38
    • 0029826535 scopus 로고    scopus 로고
    • Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains
    • Ohno, H., M.C. Fournier, G. Poy, and J.S. Bonifacino. 1996. Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains. J. Biol. Chem. 271: 29009-29015.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29009-29015
    • Ohno, H.1    Fournier, M.C.2    Poy, G.3    Bonifacino, J.S.4
  • 39
    • 0023052287 scopus 로고
    • A new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stack
    • Orci, L., B.S. Glick, and J.E. Rothman. 1986. A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell. 46:171-184.
    • (1986) Cell , vol.46 , pp. 171-184
    • Orci, L.1    Glick, B.S.2    Rothman, J.E.3
  • 42
    • 0028351154 scopus 로고
    • The TGN38 glycoprotein contains two nonoverlapping signals that mediate localization to the trans-Golgi network
    • Ponnambalam, S., C. Rabouille, J.P. Luzio, T. Nilsson, and G. Warren. 1994. The TGN38 glycoprotein contains two nonoverlapping signals that mediate localization to the trans-Golgi network. J. Cell Biol. 125:253-268.
    • (1994) J. Cell Biol. , vol.125 , pp. 253-268
    • Ponnambalam, S.1    Rabouille, C.2    Luzio, J.P.3    Nilsson, T.4    Warren, G.5
  • 43
    • 0027968347 scopus 로고
    • Overexpression of TGN38/41 leads to mislocalisation of gamma-adaptin
    • Reaves, B., and G. Banting. 1994. Overexpression of TGN38/41 leads to mislocalisation of gamma-adaptin. FEBS Lett. 351:448-456.
    • (1994) FEBS Lett. , vol.351 , pp. 448-456
    • Reaves, B.1    Banting, G.2
  • 44
    • 0025642375 scopus 로고
    • Cloning and expression of γ adaptin, a component of clathrin-coated vesicles associated with the Golgi apparatus
    • Robinson, M.S. 1990. Cloning and expression of γ adaptin, a component of clathrin-coated vesicles associated with the Golgi apparatus. J. Cell Biol. 111: 2319-2326.
    • (1990) J. Cell Biol. , vol.111 , pp. 2319-2326
    • Robinson, M.S.1
  • 45
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin A and G protein activators
    • Robinson, M.S., and T.E. Kreis. 1992. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell. 69:129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 47
    • 0029670289 scopus 로고    scopus 로고
    • Protein transport by transport vesicles
    • Rothman, J.E., and F.T. Wieland. 1996. Protein transport by transport vesicles. Science. 272:227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 48
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science. 271:1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 49
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K., and A. Wandinger-Ness. 1990. Polarized sorting in epithelia. Cell. 62:207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 50
    • 0021806048 scopus 로고
    • A new method for preparing gold probes for multiple labeling cytochemistry
    • Slot, J.W., and H.J. Geuze. 1985. A new method for preparing gold probes for multiple labeling cytochemistry. Eur. J. Cell Biol. 38:87-93.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 87-93
    • Slot, J.W.1    Geuze, H.J.2
  • 51
    • 0021955354 scopus 로고
    • Intracellular movement of cell surface rerceptors after endocytosis: Resialylation of asialo-transferrin receptor in human erythroleukemia cells
    • Snider, M.D., and O.C. Rogers. 1985. Intracellular movement of cell surface rerceptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells. J. Cell Biol. 100:826-834.
    • (1985) J. Cell Biol. , vol.100 , pp. 826-834
    • Snider, M.D.1    Rogers, O.C.2
  • 53
    • 0029610381 scopus 로고
    • Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex
    • Stinchcombe, J., D. Cutler, and C.R. Hopkins. 1995. Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex. J. Cell Biol. 131:1387-1401.
    • (1995) J. Cell Biol. , vol.131 , pp. 1387-1401
    • Stinchcombe, J.1    Cutler, D.2    Hopkins, C.R.3
  • 54
    • 0023729781 scopus 로고
    • The pathways of endocytosed transferrin and secretory protein are connected in the trans-Golgi reticulum
    • Stoorvogel, W., H.J. Geuze, J.M. Griffith, and G.J. Strous. 1988. The pathways of endocytosed transferrin and secretory protein are connected in the trans-Golgi reticulum. J. Cell Biol. 106:1821-1829.
    • (1988) J. Cell Biol. , vol.106 , pp. 1821-1829
    • Stoorvogel, W.1    Geuze, H.J.2    Griffith, J.M.3    Strous, G.J.4
  • 55
    • 0030047961 scopus 로고    scopus 로고
    • A novel class of clathrin-coated vesicles budding from endosomes
    • Stoorvogel, W., V. Oorschot, and H.J. Geuze. 1996. A novel class of clathrin-coated vesicles budding from endosomes. J. Cell Biol. 132:21-33.
    • (1996) J. Cell Biol. , vol.132 , pp. 21-33
    • Stoorvogel, W.1    Oorschot, V.2    Geuze, H.J.3
  • 56
    • 0027333415 scopus 로고
    • Signal-dependent membrane protein trafficking in the endocytic pathway
    • Trowbridge, I.S., J.F. Collawn, and C.R. Hopkins. 1993. Signal-dependent membrane protein trafficking in the endocytic pathway. Annu. Rev. Cell Biol. 9:129-161.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 129-161
    • Trowbridge, I.S.1    Collawn, J.F.2    Hopkins, C.R.3
  • 57
    • 0029129121 scopus 로고
    • Selective reentry of recycling cell surface glycoproteins to the biosynthetic pathway in human hepatocarcinoma HepG2 cells
    • Volz, B., G. Orberger, S. Porwoll, H.-P. Hauri, and R. Tauber. 1995. Selective reentry of recycling cell surface glycoproteins to the biosynthetic pathway in human hepatocarcinoma HepG2 cells. J. Cell Biol. 130:537-552.
    • (1995) J. Cell Biol. , vol.130 , pp. 537-552
    • Volz, B.1    Orberger, G.2    Porwoll, S.3    Hauri, H.-P.4    Tauber, R.5
  • 58
    • 0028301797 scopus 로고
    • Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells
    • Wagner, M., A.K. Rajasekaran, D.K. Hanzel, S. Mayor, and E. Rodriguez-Boulan. 1994. Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells. J. Cell Sci. 107:933-943.
    • (1994) J. Cell Sci. , vol.107 , pp. 933-943
    • Wagner, M.1    Rajasekaran, A.K.2    Hanzel, D.K.3    Mayor, S.4    Rodriguez-Boulan, E.5
  • 59
    • 0026716393 scopus 로고
    • Brefeldin A enhances receptor-mediated transcytosis of transferrin in filter-grown Madin-Darby canine kidney cells
    • Wan, J., M.E. Taub, D. Shah, and W.-C. Shen. 1992. Brefeldin A enhances receptor-mediated transcytosis of transferrin in filter-grown Madin-Darby canine kidney cells. J. Biol. Chem. 267:13446-13450.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13446-13450
    • Wan, J.1    Taub, M.E.2    Shah, D.3    Shen, W.-C.4
  • 61
    • 0026747939 scopus 로고
    • Monoclonal antibodies against defined epitopes of the human transferrin receptor cytoplasmic tail
    • White, S., K. Miller, C. Hopkins, and I.S. Trowbridge. 1992. Monoclonal antibodies against defined epitopes of the human transferrin receptor cytoplasmic tail. Biochim. Biophys. Acta. 1136:28-34.
    • (1992) Biochim. Biophys. Acta , vol.1136 , pp. 28-34
    • White, S.1    Miller, K.2    Hopkins, C.3    Trowbridge, I.S.4
  • 62
    • 0028875216 scopus 로고
    • Cytoplasmic coat proteins involved in endosome function
    • Whitney, J.A., M. Gomez, D. Sheff, T.E. Kreis, and I. Mellman. 1995. Cytoplasmic coat proteins involved in endosome function. Cell. 83:703-713.
    • (1995) Cell , vol.83 , pp. 703-713
    • Whitney, J.A.1    Gomez, M.2    Sheff, D.3    Kreis, T.E.4    Mellman, I.5
  • 63
    • 0026628312 scopus 로고
    • 100-kD proteins of the Golgi and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties
    • Wong, D.H., and F.M. Brodsky. 1992. 100-kD proteins of the Golgi and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties. J. Cell Biol. 117:1171-1179.
    • (1992) J. Cell Biol. , vol.117 , pp. 1171-1179
    • Wong, D.H.1    Brodsky, F.M.2
  • 64
    • 0027519431 scopus 로고
    • The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localisation
    • Wong, S.H., and W. Hong. 1993. The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localisation. J. Biol. Chem. 268:22853-22862.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22853-22862
    • Wong, S.H.1    Hong, W.2
  • 65
    • 0025943380 scopus 로고
    • Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes
    • Wood, S.A., J.E. Park, and W.J. Brown. 1991. Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes. Cell. 67:591-600.
    • (1991) Cell , vol.67 , pp. 591-600
    • Wood, S.A.1    Park, J.E.2    Brown, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.