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Volumn 1404, Issue 1-2, 1998, Pages 53-66

Regulation of membrane traffic in animal cells by COPI

Author keywords

Coated vesicle; Coatomer; COPI; Golgi complex; Membrane traffic

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; COAT PROTEIN; MEMBRANE PROTEIN;

EID: 0032516893     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(98)00046-9     Document Type: Article
Times cited : (83)

References (107)
  • 1
    • 0021738607 scopus 로고
    • Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine
    • Balch W.E., Dunphy W.G., Braell W.A., Rothman J.E. Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell. 39:1984;405-416.
    • (1984) Cell , vol.39 , pp. 405-416
    • Balch, W.E.1    Dunphy, W.G.2    Braell, W.A.3    Rothman, J.E.4
  • 2
    • 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., Glick B.S., Rothman J.E. A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell. 46:1986;171-184.
    • (1986) Cell , vol.46 , pp. 171-184
    • Orci, L.1    Glick, B.S.2    Rothman, J.E.3
  • 4
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack
    • Malhotra V., Serafini T., Orci L., Shepherd J.C., Rothman J.E. Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack. Cell. 58:1989;329-336.
    • (1989) Cell , vol.58 , pp. 329-336
    • Malhotra, V.1    Serafini, T.2    Orci, L.3    Shepherd, J.C.4    Rothman, J.E.5
  • 5
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini T., Orci L., Amherdt M., Brunner M., Kahn R.A., Rothman J.E. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell. 67:1991;239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 6
    • 0025957468 scopus 로고
    • 'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters M.G., Serafini T., Rothman J.E. 'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature. 349:1991;248-251.
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.G.1    Serafini, T.2    Rothman, J.E.3
  • 7
    • 0026034357 scopus 로고
    • β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin
    • Duden R., Griffiths G., Frank R., Argos P., Kreis T.E. β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin. Cell. 64:1991;649-665.
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Griffiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 9
    • 0025894953 scopus 로고
    • Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins
    • Kahn R.A., Kern F.G., Clark J., Gelmann E.P., Rulka C. Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins. J. Biol. Chem. 266:1991;2606-2614.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2606-2614
    • Kahn, R.A.1    Kern, F.G.2    Clark, J.3    Gelmann, E.P.4    Rulka, C.5
  • 10
    • 0028904466 scopus 로고
    • ARF proteins - The membrane traffic police
    • Boman A.L., Kahn R.A. ARF proteins - the membrane traffic police. Trends Biochem. Sci. 20:1995;147-150.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 147-150
    • Boman, A.L.1    Kahn, R.A.2
  • 12
    • 0030002357 scopus 로고    scopus 로고
    • Hep-COP, a novel human gene whose product is highly homologous to the alpha-subunit of the yeast coatomer protein complex
    • Chow V.T.K., Quek H.H. Hep-COP, a novel human gene whose product is highly homologous to the alpha-subunit of the yeast coatomer protein complex. Gene. 169:1996;223-227.
    • (1996) Gene , vol.169 , pp. 223-227
    • Chow, V.T.K.1    Quek, H.H.2
  • 13
    • 0027274897 scopus 로고
    • A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins
    • Harrison-Lavoie K.J., Lewis V.A., Hynes G.M., Collison K.S., Nutland E., Willison K.R. A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins. EMBO J. 12:1993;2847-2853.
    • (1993) EMBO J. , vol.12 , pp. 2847-2853
    • Harrison-Lavoie, K.J.1    Lewis, V.A.2    Hynes, G.M.3    Collison, K.S.4    Nutland, E.5    Willison, K.R.6
  • 16
    • 0029874257 scopus 로고    scopus 로고
    • Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway
    • Harter C., Pavel J., Coccia F., Draken E., Wegehingel S., Tschochner H., Wieland F. Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway. Proc. Natl. Acad. Sci. USA. 93:1996;1902-1906.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1902-1906
    • Harter, C.1    Pavel, J.2    Coccia, F.3    Draken, E.4    Wegehingel, S.5    Tschochner, H.6    Wieland, F.7
  • 20
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer E.J., Schmidt C.J., Nambudripad R., Smith T.F. The ancient regulatory-protein family of WD-repeat proteins. Nature. 371:1994;297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 22
    • 0029988456 scopus 로고    scopus 로고
    • δ-COP and ζ-COP, 2 coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval
    • Cosson P., Demolliere C., Hennecke S., Duden R., Letourneur F. δ-COP and ζ-COP, 2 coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval. EMBO J. 15:1996;1792-1798.
    • (1996) EMBO J. , vol.15 , pp. 1792-1798
    • Cosson, P.1    Demolliere, C.2    Hennecke, S.3    Duden, R.4    Letourneur, F.5
  • 23
    • 0028147242 scopus 로고
    • The human keratinocyte two-dimensional protein database (update 1994): Towards an integrated approach to the study of cell proliferation, differentiation and skin disease
    • Celis J.E., Rasmussen H.H., Olsen E., Madsen P., Leffers H., Honore B., Dejgaard K., Gromov P., Vorum H., Vassilev A., et al. The human keratinocyte two-dimensional protein database (update 1994): towards an integrated approach to the study of cell proliferation, differentiation and skin disease. Electrophoresis. 15:1994;1349-1458.
    • (1994) Electrophoresis , vol.15 , pp. 1349-1458
    • Celis, J.E.1    Rasmussen, H.H.2    Olsen, E.3    Madsen, P.4    Leffers, H.5    Honore, B.6    Dejgaard, K.7    Gromov, P.8    Vorum, H.9    Vassilev, A.10
  • 24
    • 0029924185 scopus 로고    scopus 로고
    • Biochemical heterogeneity and phosphorylation of coatomer subunits
    • Sheff D., Lowe M., Kreis T.E., Mellman I. Biochemical heterogeneity and phosphorylation of coatomer subunits. J. Biol. Chem. 271:1996;7230-7236.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7230-7236
    • Sheff, D.1    Lowe, M.2    Kreis, T.E.3    Mellman, I.4
  • 25
    • 0029623181 scopus 로고
    • In vitro assembly and disassembly of coatomer
    • Lowe M., Kreis T.E. In vitro assembly and disassembly of coatomer. J. Biol. Chem. 270:1995;31364-31371.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31364-31371
    • Lowe, M.1    Kreis, T.E.2
  • 26
    • 0032478277 scopus 로고    scopus 로고
    • Reversible dissociation of coatomer: Functional characterization of a β/δ-COP subcomplex
    • Pavel J., Harter C., Wieland F.T. Reversible dissociation of coatomer: functional characterization of a β/δ-COP subcomplex. Proc. Natl. Acad. Sci. USA. 95:1998;2140-2145.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2140-2145
    • Pavel, J.1    Harter, C.2    Wieland, F.T.3
  • 27
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson P., Letourneur F. Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science. 263:1994;1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 28
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler K., Veit M., Stamnes M.A., Rothman J.E. Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science. 273:1996;1396-1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 29
    • 0029844218 scopus 로고    scopus 로고
    • In vivo assembly of coatomer, the COP-I coat precursor
    • Lowe M., Kreis T.E. In vivo assembly of coatomer, the COP-I coat precursor. J. Biol. Chem. 271:1996;30725-30730.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30725-30730
    • Lowe, M.1    Kreis, T.E.2
  • 30
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein β-COP to Golgi membranes
    • Donaldson J.G., Cassel D., Kahn R.A., Klausner R.D. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein β-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA. 89:1992;6408-6412.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 31
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer D.J., Helms J.B., Beckers C.J.M., Orci L., Rothman J.E. Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J. Biol. Chem. 268:1993;12083-12089.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12083-12089
    • Palmer, D.J.1    Helms, J.B.2    Beckers, C.J.M.3    Orci, L.4    Rothman, J.E.5
  • 32
    • 0026327556 scopus 로고
    • Binding of ARF and β-COP to Golgi membranes: Possible regulation by a trimeric G protein
    • Donaldson J.G., Kahn R.A., Lippincott-Schwartz J., Klausner R.D. Binding of ARF and β-COP to Golgi membranes: possible regulation by a trimeric G protein. Science. 254:1991;1197-1199.
    • (1991) Science , vol.254 , pp. 1197-1199
    • Donaldson, J.G.1    Kahn, R.A.2    Lippincott-Schwartz, J.3    Klausner, R.D.4
  • 33
    • 0025996803 scopus 로고
    • Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins
    • Kahn R.A. Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins. J. Biol. Chem. 266:1991;15595-15597.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15595-15597
    • Kahn, R.A.1
  • 34
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson J.G., Finazzi D., Klausner R.D. Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature. 360:1992;350-352.
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 35
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyzes exchange of guanine-nucleotide bound to ARF
    • Helms J.B., Rothman J.E. Inhibition by brefeldin A of a Golgi membrane enzyme that catalyzes exchange of guanine-nucleotide bound to ARF. Nature. 360:1992;352-354.
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 36
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes
    • Misumi Y., Misumi Y., Miki K., Takatsuki A., Tamura G., Ikehara Y. Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes. J. Biol. Chem. 261:1986;11398-11403.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Misumi, Y.2    Miki, K.3    Takatsuki, A.4    Tamura, G.5    Ikehara, Y.6
  • 37
    • 0029758214 scopus 로고    scopus 로고
    • P619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins
    • Rosa J.L., Casaroli-Marano R.P., Buckler A.J., Vilaro S., Barbacid M. p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins. EMBO J. 15:1996;4262-4273.
    • (1996) EMBO J. , vol.15 , pp. 4262-4273
    • Rosa, J.L.1    Casaroli-Marano, R.P.2    Buckler, A.J.3    Vilaro, S.4    Barbacid, M.5
  • 39
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on arf mediated by yeast gea1 protein
    • Peyroche A., Paris S., Jackson C.L. Nucleotide exchange on arf mediated by yeast gea1 protein. Nature. 384:1996;479-481.
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 41
    • 0030013233 scopus 로고    scopus 로고
    • Evidence that phospholipase-D mediates ADP-ribosylation factor-dependent formation Golgi coated vesicles
    • Ktistakis N.T., Brown H.A., Waters M.G., Sternweis P.C., Roth M.G. Evidence that phospholipase-D mediates ADP-ribosylation factor-dependent formation Golgi coated vesicles. J. Cell Biol. 134:1996;295-306.
    • (1996) J. Cell Biol. , vol.134 , pp. 295-306
    • Ktistakis, N.T.1    Brown, H.A.2    Waters, M.G.3    Sternweis, P.C.4    Roth, M.G.5
  • 42
    • 0029065704 scopus 로고
    • Phospholipase-D is present on Golgi-enriched membranes and its activation by ADP-ribosylation factor is sensitive to brefeldin A
    • Ktistakis N.T., Brown H.A., Sternweis P.C., Roth M.G. Phospholipase-D is present on Golgi-enriched membranes and its activation by ADP-ribosylation factor is sensitive to brefeldin A. Proc. Natl. Acad. Sci. USA. 92:1995;4952-4956.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4952-4956
    • Ktistakis, N.T.1    Brown, H.A.2    Sternweis, P.C.3    Roth, M.G.4
  • 43
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown H.A., Gutowski S., Moomaw C.R., Slaughter C., Sternweiss P.C. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell. 75:1993;1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweiss, P.C.5
  • 45
  • 46
    • 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., Kreis T.E. Recruitment of Coat-proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin A and G-protein activators. Cell. 69:1992;129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 47
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes M.A., Rothman J.E. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell. 73:1993;999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 48
    • 0030881255 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment
    • West M.A., Bright N.A., Robinson M.S. The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment. J. Cell Biol. 138:1997;1239-1254.
    • (1997) J. Cell Biol. , vol.138 , pp. 1239-1254
    • West, M.A.1    Bright, N.A.2    Robinson, M.S.3
  • 49
    • 0029416828 scopus 로고
    • The ARF1 GTPase-activating protein - zinc-finger motif and Golgi complex localization
    • Cukierman E., Huber I., Rotman M., Cassel D. The ARF1 GTPase-activating protein - zinc-finger motif and Golgi complex localization. Science. 270:1995;1999-2002.
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 50
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson T., Jackson M., Peterson P.A. Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell. 58:1989;707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.A.3
  • 51
    • 0030868677 scopus 로고    scopus 로고
    • Interaction of coatomer with aminoglycoside antibiotics: Evidence that coatomer has at least two dilysine binding sites
    • Hudson R.T., Draper R.K. Interaction of coatomer with aminoglycoside antibiotics: evidence that coatomer has at least two dilysine binding sites. Mol. Biol. Cell. 8:1997;1901-1910.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1901-1910
    • Hudson, R.T.1    Draper, R.K.2
  • 52
    • 0030995064 scopus 로고    scopus 로고
    • P53/58 binds COPI and is required for selective transport through the early secretory pathway
    • Tisdale E.J., Plutner H., Matteson J., Balch W.E. p53/58 binds COPI and is required for selective transport through the early secretory pathway. J. Cell Biol. 137:1997;581-593.
    • (1997) J. Cell Biol. , vol.137 , pp. 581-593
    • Tisdale, E.J.1    Plutner, H.2    Matteson, J.3    Balch, W.E.4
  • 53
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller F., Singer Kruger B., Schroder S., Kruger U., Barlowe C., Riezman H. The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J. 14:1995;1329-1339.
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 56
    • 0029910214 scopus 로고    scopus 로고
    • Erv25p, a component of copii-coated vesicles, forms a complex with emp24p that is required for efficient endoplasmic-reticulum to Golgi transport
    • Belden W.J., Barlowe C. Erv25p, a component of copii-coated vesicles, forms a complex with emp24p that is required for efficient endoplasmic-reticulum to Golgi transport. J. Biol. Chem. 271:1996;26939-26946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26939-26946
    • Belden, W.J.1    Barlowe, C.2
  • 57
    • 0030800703 scopus 로고    scopus 로고
    • Biogenesis of COPI-coated transport vesicles
    • Nickel W., Wieland F.T. Biogenesis of COPI-coated transport vesicles. FEBS Lett. 413:1997;395-400.
    • (1997) FEBS Lett. , vol.413 , pp. 395-400
    • Nickel, W.1    Wieland, F.T.2
  • 58
    • 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., Griffiths G., Hoflack B. 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. 271:1996;2162-2170.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2162-2170
    • Le Borgne, R.1    Griffiths, G.2    Hoflack, B.3
  • 59
    • 0027291429 scopus 로고
    • Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • Orci L., Palmer D.J., Amherdt M., Rothman J.E. Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature. 364:1993;732-734.
    • (1993) Nature , vol.364 , pp. 732-734
    • Orci, L.1    Palmer, D.J.2    Amherdt, M.3    Rothman, J.E.4
  • 60
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J.E. Mechanisms of intracellular protein transport. Nature. 372:1994;55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 61
    • 0024435355 scopus 로고
    • Fatty acyl-coenzyme A is required for budding of transport vesicles from Golgi cisternae
    • Pfanner N., Orci L., Glick B.S., Amherdt M., Arden S.R., Malhotra V., Rothman J.E. Fatty acyl-coenzyme A is required for budding of transport vesicles from Golgi cisternae. Cell. 59:1989;95-102.
    • (1989) Cell , vol.59 , pp. 95-102
    • Pfanner, N.1    Orci, L.2    Glick, B.S.3    Amherdt, M.4    Arden, S.R.5    Malhotra, V.6    Rothman, J.E.7
  • 64
    • 0027328703 scopus 로고
    • ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif
    • Schindler R., Itin C., Zerial M., Lottspeich F., Hauri H.P. ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif. Eur. J. Cell Biol. 61:1993;1-9.
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 1-9
    • Schindler, R.1    Itin, C.2    Zerial, M.3    Lottspeich, F.4    Hauri, H.P.5
  • 65
    • 0028926420 scopus 로고
    • ERGIC-53, a membrane-protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells
    • Arar C., Carpentier V., Lecaer J.P., Monsigny M., Legrand A., Roche A.C. ERGIC-53, a membrane-protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells. J. Biol. Chem. 270:1995;3551-3553.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3551-3553
    • Arar, C.1    Carpentier, V.2    Lecaer, J.P.3    Monsigny, M.4    Legrand, A.5    Roche, A.C.6
  • 66
    • 0029876344 scopus 로고    scopus 로고
    • ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins
    • Itin C., Roche A.C., Monsigny M., Hauri H.P. ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins. Mol. Biol. Cell. 7:1996;483-493.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 483-493
    • Itin, C.1    Roche, A.C.2    Monsigny, M.3    Hauri, H.P.4
  • 67
    • 0029098968 scopus 로고
    • Targeting of protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway
    • Itin C., Schindler R., Hauri H.P. Targeting of protein ERGIC-53 to the ER/ERGIC/cis-Golgi recycling pathway. J. Cell Biol. 131:1995;57-67.
    • (1995) J. Cell Biol. , vol.131 , pp. 57-67
    • Itin, C.1    Schindler, R.2    Hauri, H.P.3
  • 68
    • 0030868332 scopus 로고    scopus 로고
    • P23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway
    • Nickel W., Sohn K., Bunning C., Wieland F.T. p23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway. Proc. Natl. Acad. Sci. USA. 94:1997;11393-11398.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11393-11398
    • Nickel, W.1    Sohn, K.2    Bunning, C.3    Wieland, F.T.4
  • 69
    • 0029838658 scopus 로고    scopus 로고
    • Sorting by COP I-coated vesicles under interphase and mitotic conditions
    • Sönnichsen B., Watson R., Clausen H., Misteli T., Warren G. Sorting by COP I-coated vesicles under interphase and mitotic conditions. J. Cell Biol. 134:1996;1411-1425.
    • (1996) J. Cell Biol. , vol.134 , pp. 1411-1425
    • Sönnichsen, B.1    Watson, R.2    Clausen, H.3    Misteli, T.4    Warren, G.5
  • 70
    • 0031826012 scopus 로고    scopus 로고
    • Three distinct steps in transport of vesicular stomatitis virus glycoprotein from the ER to the cell surface in vivo with differential sensitivities to GTPγS
    • in press
    • R. Pepperkok, M. Lowe, B. Burke, T.E. Kreis, Three distinct steps in transport of vesicular stomatitis virus glycoprotein from the ER to the cell surface in vivo with differential sensitivities to GTPγS, J. Cell Sci. (1998) in press.
    • (1998) J. Cell Sci.
    • Pepperkok, R.1    Lowe, M.2    Burke, B.3    Kreis, T.E.4
  • 71
    • 0027179841 scopus 로고
    • Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex
    • De Matteis A., Santini G., Kahn R.A., Di T.G., Luini A. Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex. Nature. 364:1993;818-821.
    • (1993) Nature , vol.364 , pp. 818-821
    • De Matteis, A.1    Santini, G.2    Kahn, R.A.3    Di, T.G.4    Luini, A.5
  • 72
    • 0028290272 scopus 로고
    • Aluminum fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes
    • Finazzi D., Cassel D., Donaldson J.G., Klausner R.D. Aluminum fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes. J. Biol. Chem. 269:1994;13325-13330.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13325-13330
    • Finazzi, D.1    Cassel, D.2    Donaldson, J.G.3    Klausner, R.D.4
  • 73
    • 0028329279 scopus 로고
    • Cytosolic ARFs are required for vesicle formation but not for cell-free intra-Golgi transport: Evidence for coated vesicle-independent transport
    • Taylor T.C., Kanstein M., Weidman P., Melançon P. Cytosolic ARFs are required for vesicle formation but not for cell-free intra-Golgi transport: Evidence for coated vesicle-independent transport. Mol. Biol. Cell. 5:1994;237-252.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 237-252
    • Taylor, T.C.1    Kanstein, M.2    Weidman, P.3    Melançon, P.4
  • 75
    • 0030938305 scopus 로고    scopus 로고
    • Dissociation of coatomer from membranes is required for brefeldin A-induced transfer of Golgi enzymes to the endoplasmic reticulum
    • Scheel J., Pepperkok R., Lowe M., Griffiths G., Kreis T.E. Dissociation of coatomer from membranes is required for brefeldin A-induced transfer of Golgi enzymes to the endoplasmic reticulum. J. Cell Biol. 137:1997;319-333.
    • (1997) J. Cell Biol. , vol.137 , pp. 319-333
    • Scheel, J.1    Pepperkok, R.2    Lowe, M.3    Griffiths, G.4    Kreis, T.E.5
  • 76
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman J.E., Orci L. Molecular dissection of the secretory pathway. Nature. 355:1992;409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 77
    • 0028661187 scopus 로고
    • About turn for the COPs
    • Pelham H.R.B. About turn for the COPs. Cell. 79:1994;1125-1127.
    • (1994) Cell , vol.79 , pp. 1125-1127
    • Pelham, H.R.B.1
  • 78
    • 0001805181 scopus 로고
    • Golgi apparatus and slime secretion in plants: The early implications and recent models of membrane traffic
    • Schnepf E. Golgi apparatus and slime secretion in plants: the early implications and recent models of membrane traffic. Protoplasma. 172:1993;3-11.
    • (1993) Protoplasma , vol.172 , pp. 3-11
    • Schnepf, E.1
  • 79
    • 0030753006 scopus 로고    scopus 로고
    • Variations on the intracellular transport theme: Maturing cisternae and trafficking tubules
    • Mironov A.A., Weidman P., Luini A. Variations on the intracellular transport theme: maturing cisternae and trafficking tubules. J. Cell Biol. 138:1997;481-484.
    • (1997) J. Cell Biol. , vol.138 , pp. 481-484
    • Mironov, A.A.1    Weidman, P.2    Luini, A.3
  • 80
    • 0031559885 scopus 로고    scopus 로고
    • A cisternal maturation mechanism can explain the asymmetry of the Golgi stack
    • Glick B.S., Elston T., Oster G. A cisternal maturation mechanism can explain the asymmetry of the Golgi stack. FEBS Lett. 414:1997;177-181.
    • (1997) FEBS Lett. , vol.414 , pp. 177-181
    • Glick, B.S.1    Elston, T.2    Oster, G.3
  • 82
    • 0031552875 scopus 로고    scopus 로고
    • Membrane-transport - green light for Golgi traffic
    • Pelham H.R.B. Membrane-transport - green light for Golgi traffic. Nature. 389:1997;17-18.
    • (1997) Nature , vol.389 , pp. 17-18
    • Pelham, H.R.B.1
  • 85
    • 0030803090 scopus 로고    scopus 로고
    • Does COPI go both ways?
    • Schekman R., Mellman I. Does COPI go both ways? Cell. 90:1997;197-200.
    • (1997) Cell , vol.90 , pp. 197-200
    • Schekman, R.1    Mellman, I.2
  • 86
    • 0030742746 scopus 로고    scopus 로고
    • Membrane dynamics at the endoplasmic-reticulum Golgi interface
    • Bannykh S.I., Balch W.E. Membrane dynamics at the endoplasmic-reticulum Golgi interface. J. Cell Biol. 138:1997;1-4.
    • (1997) J. Cell Biol. , vol.138 , pp. 1-4
    • Bannykh, S.I.1    Balch, W.E.2
  • 87
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales S.J., Pepperkok R., Kreis T.E. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell. 90:1997;1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 88
    • 0027499531 scopus 로고
    • β-COP localizes mainly to the cis-Golgi side in exocrine pancreas
    • Oprins A., Duden R., Kreis T.E., Geuze H.J., Slot J.W. β-COP localizes mainly to the cis-Golgi side in exocrine pancreas. J. Cell Biol. 121:1993;49-59.
    • (1993) J. Cell Biol. , vol.121 , pp. 49-59
    • Oprins, A.1    Duden, R.2    Kreis, T.E.3    Geuze, H.J.4    Slot, J.W.5
  • 89
    • 0028984235 scopus 로고
    • Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN
    • Griffiths G., Pepperkok R., Locker J.K., Kreis T.E. Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN. J. Cell Sci. 108:1995;2839-2856.
    • (1995) J. Cell Sci. , vol.108 , pp. 2839-2856
    • Griffiths, G.1    Pepperkok, R.2    Locker, J.K.3    Kreis, T.E.4
  • 90
    • 0028971172 scopus 로고
    • Sequential coupling between COPII and COPI vesicle coats in endoplasmic-reticulum to Golgi transport
    • Aridor M., Bannykh S.I., Rowe T., Balch W.E. Sequential coupling between COPII and COPI vesicle coats in endoplasmic-reticulum to Golgi transport. J. Cell Biol. 131:1995;875-893.
    • (1995) J. Cell Biol. , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 93
    • 0027220591 scopus 로고
    • β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok R., Scheel J., Horstmann H., Hauri H.P., Griffiths G., Kreis T.E. β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell. 74:1993;71-82.
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 94
    • 0027165412 scopus 로고
    • β-COP is essential for transport of protein from the endoplasmic-reticulum to the Golgi in vitro
    • Peter F., Plutner H., Zhu H.Y., Kreis T.E., Balch W.E. β-COP is essential for transport of protein from the endoplasmic-reticulum to the Golgi in vitro. J. Cell Biol. 122:1993;1155-1167.
    • (1993) J. Cell Biol. , vol.122 , pp. 1155-1167
    • Peter, F.1    Plutner, H.2    Zhu, H.Y.3    Kreis, T.E.4    Balch, W.E.5
  • 95
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic-reticulum to Golgi transport and trigger disassembly of the Golgi-apparatus
    • Dascher C., Balch W.E. Dominant inhibitory mutants of ARF1 block endoplasmic-reticulum to Golgi transport and trigger disassembly of the Golgi-apparatus. J. Biol. Chem. 269:1994;1437-1448.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 97
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis M.J., Pelham H.R. SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell. 85:1996;205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.2
  • 98
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman R., Orci L. Coat proteins and vesicle budding. Science. 271:1996;1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 99
    • 0029836930 scopus 로고    scopus 로고
    • COP II vesicles derived from mammalian endoplasmic-reticulum microsomes recruit COP I
    • Rowe T., Aridor M., McCaffery J.M., Plutner H., Nuoffer C., Balch W.E. COP II vesicles derived from mammalian endoplasmic-reticulum microsomes recruit COP I. J. Cell Biol. 135:1996;895-911.
    • (1996) J. Cell Biol. , vol.135 , pp. 895-911
    • Rowe, T.1    Aridor, M.2    McCaffery, J.M.3    Plutner, H.4    Nuoffer, C.5    Balch, W.E.6
  • 100
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson M.R., Nilsson T., Peterson P.A. Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121:1993;317-333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 101
  • 102
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12:1996;575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 103
    • 0028875216 scopus 로고
    • Cytoplasmic coated proteins involved in endosome function
    • Whitney J.A., Gomez M., Sheff D., Kreis T.E., Mellman I. Cytoplasmic coated proteins involved in endosome function. Cell. 83:1995;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
  • 104
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal β-COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • Aniento F., Gu F., Parton R.G., Gruenberg J. An endosomal β-COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes. J. Cell Biol. 133:1996;29-41.
    • (1996) J. Cell Biol. , vol.133 , pp. 29-41
    • Aniento, F.1    Gu, F.2    Parton, R.G.3    Gruenberg, J.4
  • 105
    • 0028264318 scopus 로고
    • Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by ε-COP
    • Guo Q., Vasile E., Krieger M. Disruptions in Golgi structure and membrane traffic in a conditional lethal mammalian cell mutant are corrected by ε-COP. J. Cell Biol. 125:1994;1213-1224.
    • (1994) J. Cell Biol. , vol.125 , pp. 1213-1224
    • Guo, Q.1    Vasile, E.2    Krieger, M.3
  • 106
    • 0031425955 scopus 로고    scopus 로고
    • Inhibition of endosome function in chinese hamster ovary (CHO) cells bearing temperature-sensitive defect in {epsilon}-coat proteins (COP)
    • Daro E., Sheff D., Gomez M., Kreis T.E., Mellman I. Inhibition of endosome function in chinese hamster ovary (CHO) cells bearing temperature-sensitive defect in {epsilon}-coat proteins (COP). J. Cell Biol. 139:1997;1747-1759.
    • (1997) J. Cell Biol. , vol.139 , pp. 1747-1759
    • Daro, E.1    Sheff, D.2    Gomez, M.3    Kreis, T.E.4    Mellman, I.5
  • 107
    • 85058247691 scopus 로고    scopus 로고
    • Identification of novel coatomer and adaptin related proteins
    • Whitney J.A., Kreis T.E. Identification of novel coatomer and adaptin related proteins. Mol. Biol. Cell. 7:1996;79a.
    • (1996) Mol. Biol. Cell , vol.7
    • Whitney, J.A.1    Kreis, T.E.2


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