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Volumn 139, Issue 5, 1997, Pages 1157-1168

The mammalian protein (rbet1) homologous to yeast Bet1p is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus

Author keywords

[No Author keywords available]

Indexed keywords

DOCKING PROTEIN; EGTAZIC ACID; GUANINE NUCLEOTIDE BINDING PROTEIN; MANNOSIDASE; N ETHYLMALEIMIDE; NOCODAZOLE; RECEPTOR PROTEIN; RECOMBINANT PROTEIN;

EID: 1842335138     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.5.1157     Document Type: Article
Times cited : (58)

References (74)
  • 1
    • 0028971172 scopus 로고
    • Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport
    • Aridor, M., S.I. Bannykh, T. Rowe, and W.E. Balch. 1995. Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J. Cell Biol. 131:875-893.
    • (1995) J. Cell Biol. , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 2
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • Balch, W.E., J.M. McCaffery, H. Plunter, and M.G. Farquhar. 1994. Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell. 77:841-852.
    • (1994) Cell , vol.77 , pp. 841-852
    • Balch, W.E.1    McCaffery, J.M.2    Plunter, H.3    Farquhar, M.G.4
  • 3
    • 0027997974 scopus 로고
    • Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains
    • Banfield, D.K., M.J. Lewis, C. Rabouille, G. Warren, and H.R.B. Pelham. 1994. Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains. J. Cell Biol. 127:357-371.
    • (1994) J. Cell Biol. , vol.127 , pp. 357-371
    • Banfield, D.K.1    Lewis, M.J.2    Rabouille, C.3    Warren, G.4    Pelham, H.R.B.5
  • 4
    • 0030742746 scopus 로고    scopus 로고
    • Membrane dynamics at the endoplasmic reticulum-Golgi interface
    • Bannykh, S.I., and W.E. Balch. 1997. Membrane dynamics at the endoplasmic reticulum-Golgi interface. J. Cell Biol. 138:1-4.
    • (1997) J. Cell Biol. , vol.138 , pp. 1-4
    • Bannykh, S.I.1    Balch, W.E.2
  • 5
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • Bannykh, S.I., T. Rowe, and W.E. Balch. 1996. The organization of endoplasmic reticulum export complexes. J. Cell Biol. 135:19-35.
    • (1996) J. Cell Biol. , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 6
    • 0023653298 scopus 로고
    • Semi-intact cells permeable to macromolecules: Use in reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex
    • Beckers, C.J.M., D.S. Keller, and W.E. Balch. 1987. Semi-intact cells permeable to macromolecules: use in reconstitution of protein transport from the endoplasmic reticulum to the Golgi complex. Cell. 50:523-534.
    • (1987) Cell , vol.50 , pp. 523-534
    • Beckers, C.J.M.1    Keller, D.S.2    Balch, W.E.3
  • 7
    • 0029954687 scopus 로고    scopus 로고
    • A new syntaxin family member implicated in targeting of intracellular transport vesicle
    • Bock, J.B., R.C. Lin, and R.H. Scheller. 1996. A new syntaxin family member implicated in targeting of intracellular transport vesicle. J. Biol. Chem. 271: 17961-17965.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17961-17965
    • Bock, J.B.1    Lin, R.C.2    Scheller, R.H.3
  • 8
    • 0024322074 scopus 로고
    • Palmitylation of viral membrane glycoprotein takes place after exit from the endoplasmic reticulum
    • Bonatti, S., G. Migliaccio, and K. Simons. 1989. Palmitylation of viral membrane glycoprotein takes place after exit from the endoplasmic reticulum. J. Biol. Chem. 264:12590-12595.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12590-12595
    • Bonatti, S.1    Migliaccio, G.2    Simons, K.3
  • 9
    • 0025359065 scopus 로고
    • SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • Clary, D.O., I.C. Griff, and J.E. Rothman. 1990. SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell. 61:709-721.
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.O.1    Griff, I.C.2    Rothman, J.E.3
  • 10
    • 0025977723 scopus 로고
    • Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily
    • Dascher, C., R. Ossig, D. Gallwitz, and H.D. Schmitt. 1991. Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Mol. Cell. Biol. 11:872-885.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 872-885
    • Dascher, C.1    Ossig, R.2    Gallwitz, D.3    Schmitt, H.D.4
  • 11
    • 0028028178 scopus 로고
    • Syntaxin 5 regulates endoplasmic reticulum to Golgi transport
    • Dascher, C., J. Matteson, and W.E. Balch. 1994. Syntaxin 5 regulates endoplasmic reticulum to Golgi transport. J. Biol. Chem. 269:29363-29366.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29363-29366
    • Dascher, C.1    Matteson, J.2    Balch, W.E.3
  • 12
    • 0027416645 scopus 로고
    • Differential inhibition of multiple vesicular transport steps between the endoplasmic reticulum and trans-Golgi network
    • Davidson, H.W., and W.E. Balch. 1993. Differential inhibition of multiple vesicular transport steps between the endoplasmic reticulum and trans-Golgi network. J. Biol. Chem. 268:4216-4226.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4216-4226
    • Davidson, H.W.1    Balch, W.E.2
  • 13
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick, S., and R. Jahn. 1994. Vesicle fusion from yeast to man. Nature. 370:191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 14
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham, T.R., and S.D. Emr. 1991. Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol. 114:207-218.
    • (1991) J. Cell Biol. , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 15
    • 0026692898 scopus 로고
    • The yeast SEC17 gene product is functionally equivalent to mammalian α-SNAP protein
    • Griff, I.C., R. Schekman, J.E. Rothman, and C.A. Kaiser. 1992. The yeast SEC17 gene product is functionally equivalent to mammalian α-SNAP protein. J. Biol. Chem. 267:12106-12115.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12106-12115
    • Griff, I.C.1    Schekman, R.2    Rothman, J.E.3    Kaiser, C.A.4
  • 17
    • 0028984235 scopus 로고
    • Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN
    • Griffiths, G., R. Pepperkok, J. Krijnse-Locker, and T.E. Kreis. 1995. Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN. J. Cell Sci. 108:2839-2856.
    • (1995) J. Cell Sci. , vol.108 , pp. 2839-2856
    • Griffiths, G.1    Pepperkok, R.2    Krijnse-Locker, J.3    Kreis, T.E.4
  • 18
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan, K., and J.E. Dixon. 1991. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192:262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.1    Dixon, J.E.2
  • 19
    • 0026756118 scopus 로고
    • SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex
    • Hardwick, K.G., and H.R.B. Pelham. 1992. SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J. Cell Biol. 119:513-521.
    • (1992) J. Cell Biol. , vol.119 , pp. 513-521
    • Hardwick, K.G.1    Pelham, H.R.B.2
  • 20
    • 0029864178 scopus 로고    scopus 로고
    • Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus
    • Hay, J.C., H. Harald, and R.H. Scheller. 1996. Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus. J. Biol. Chem. 271:5671-5679.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5671-5679
    • Hay, J.C.1    Harald, H.2    Scheller, R.H.3
  • 21
    • 0030890594 scopus 로고    scopus 로고
    • Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
    • Hay, J.C., D.S. Chao, C.S. Kuo, and R.H. Scheller. 1997. Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Cell. 89:147-158.
    • (1997) Cell , vol.89 , pp. 147-158
    • Hay, J.C.1    Chao, D.S.2    Kuo, C.S.3    Scheller, R.H.4
  • 23
    • 0027580922 scopus 로고
    • Protein trafficking along the exocytotic pathway
    • Hong, W., and B.L. Tang, 1993. Protein trafficking along the exocytotic pathway. Bioassay. 15:231-238.
    • (1993) Bioassay , vol.15 , pp. 231-238
    • Hong, W.1    Tang, B.L.2
  • 24
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G. Donaldson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 25
    • 0028069572 scopus 로고
    • Characterization of the budding compartment of the mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step
    • Krijnse-Locker, J., M. Ericsson, P.J.M. Rottier, and G. Griffiths. 1994. Characterization of the budding compartment of the mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. J. Cell Biol. 124:55-70.
    • (1994) J. Cell Biol. , vol.124 , pp. 55-70
    • Krijnse-Locker, J.1    Ericsson, M.2    Rottier, P.J.M.3    Griffiths, G.4
  • 26
    • 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
  • 27
    • 0027535384 scopus 로고
    • Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus
    • Lippincott-Schwartz, J. 1993. Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus. Trends Cell Biol. 3:81-88.
    • (1993) Trends Cell Biol. , vol.3 , pp. 81-88
    • Lippincott-Schwartz, J.1
  • 29
    • 0026777411 scopus 로고
    • Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex
    • Lotti, L.V., M.R. Torrisi, M.C. Pascale, and S. Bonatti. 1992. Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex. J. Cell Biol. 118:43-50.
    • (1992) J. Cell Biol. , vol.118 , pp. 43-50
    • Lotti, L.V.1    Torrisi, M.R.2    Pascale, M.C.3    Bonatti, S.4
  • 30
    • 0030060309 scopus 로고    scopus 로고
    • The mammalian ARF-like protein 1 (Ar11) is associated with the Golgi complex
    • Lowe, S.L., S.H. Wong, and W. Hong. 1996. The mammalian ARF-like protein 1 (Ar11) is associated with the Golgi complex. J. Cell Sci. 109:209-220.
    • (1996) J. Cell Sci. , vol.109 , pp. 209-220
    • Lowe, S.L.1    Wong, S.H.2    Hong, W.3
  • 31
    • 0030062831 scopus 로고    scopus 로고
    • Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes
    • Lupashin, V.V., S. Hamamoto, and R.W. Schekman. 1996. Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes. J. Cell Biol. 132:277-289.
    • (1996) J. Cell Biol. , vol.132 , pp. 277-289
    • Lupashin, V.V.1    Hamamoto, S.2    Schekman, R.W.3
  • 32
    • 0026325913 scopus 로고
    • Isolation, characterization, and expression of cDNAs encoding murine α-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans
    • Moreman, K.W., and P.W. Robbins. 1991. Isolation, characterization, and expression of cDNAs encoding murine α-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans. J. Cell Biol. 115: 1521-1534.
    • (1991) J. Cell Biol. , vol.115 , pp. 1521-1534
    • Moreman, K.W.1    Robbins, P.W.2
  • 34
    • 0025282485 scopus 로고
    • BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex
    • Newman, A.P., J. Shim, and S. Ferro-Novick. 1990. BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Mol. Cell. Biol. 10: 3405-3414.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3405-3414
    • Newman, A.P.1    Shim, J.2    Ferro-Novick, S.3
  • 35
    • 0028239912 scopus 로고
    • GTPases: Multifunctional molecular switches regulating vesicular traffic
    • Nuoffer, C., and W.E. Balch. 1994. GTPases: multifunctional molecular switches regulating vesicular traffic. Annu. Rev. Biochem. 63:949-990.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 949-990
    • Nuoffer, C.1    Balch, W.E.2
  • 36
    • 0027499531 scopus 로고
    • β-COP localizes mainly to the cis-Golgi side in exocrine pancreas
    • Oprins, A, R. Duden, T.E. Kreis, H.J. Geuze, and J.W. Slot. 1993. β-COP localizes mainly to the cis-Golgi side in exocrine pancreas. J. Cell Biol. 121:49-59.
    • (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
  • 38
    • 0025891541 scopus 로고
    • The yeast SLY genes products, suppressors of defects in the essential GTP-bind-ing Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport
    • Ossig, R., C. Dascher, H.-H. Trepte, H.D. Schmitt, and D. Gallwitz. 1991. The yeast SLY genes products, suppressors of defects in the essential GTP-bind-ing Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell Biol. 11:2980-2993.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 2980-2993
    • Ossig, R.1    Dascher, C.2    Trepte, H.-H.3    Schmitt, H.D.4    Gallwitz, D.5
  • 40
    • 0016785996 scopus 로고
    • Intracellular aspects of the processing of protein synthesis
    • Palade, G.E. 1975. Intracellular aspects of the processing of protein synthesis. Science (Wash. DC). 189:347-354.
    • (1975) Science (Wash. DC) , vol.189 , pp. 347-354
    • Palade, G.E.1
  • 41
    • 0029752048 scopus 로고    scopus 로고
    • Transport vesicle docking: SNAREs and associates
    • Pfeffer, S.R. 1996. Transport vesicle docking: SNAREs and associates. Annu. Rev. Cell Biol. Dev. Biol. 12:441-161.
    • (1996) Annu. Rev. Cell Biol. Dev. Biol. , vol.12 , pp. 441-1161
    • Pfeffer, S.R.1
  • 44
    • 0026439921 scopus 로고
    • Morphological analysis of protein transport from the ER to the Golgi membrane in digitonin-permeabilized cells: Role of the p58 containing compartment
    • Plutner, H., H.W. Davidson, J. Saraste, and W.E. Balch. 1992. Morphological analysis of protein transport from the ER to the Golgi membrane in digitonin-permeabilized cells: role of the p58 containing compartment. J. Cell Biol. 119:1097-1116.
    • (1992) J. Cell Biol. , vol.119 , pp. 1097-1116
    • Plutner, H.1    Davidson, H.W.2    Saraste, J.3    Balch, W.E.4
  • 46
    • 0025775567 scopus 로고
    • Distinct biochemical requirements for budding, targeting, and fusion of ER-derived transport vesicles
    • Rexach, M.F., and R.W. Schekman. 1991. Distinct biochemical requirements for budding, targeting, and fusion of ER-derived transport vesicles. J. Cell Biol. 114:219-229.
    • (1991) J. Cell Biol. , vol.114 , pp. 219-229
    • Rexach, M.F.1    Schekman, R.W.2
  • 47
    • 0027965738 scopus 로고
    • Characterization of endoplasmic reticulum-derived transport vesicles
    • Rexach, M.F., M. Latterich, and R.W. Schekman. 1994. Characterization of endoplasmic reticulum-derived transport vesicles. J. Cell Biol. 126:1133-1148.
    • (1994) J. Cell Biol. , vol.126 , pp. 1133-1148
    • Rexach, M.F.1    Latterich, M.2    Schekman, R.W.3
  • 48
    • 0021135281 scopus 로고
    • Associations of elements of the Golgi apparatus with microtubule
    • Rogalski, A.A., and S.J. Singer. 1984. Associations of elements of the Golgi apparatus with microtubule. J. Cell Biol. 99:1092-1100.
    • (1984) J. Cell Biol. , vol.99 , pp. 1092-1100
    • Rogalski, A.A.1    Singer, S.J.2
  • 49
    • 0029836930 scopus 로고    scopus 로고
    • COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI
    • Rowe, T., M. Aridor, J.M. McCaffery, H. Plutner, C. Nuoffer, and W.E. Balch. 1996. COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI. J. Cell Biol. 135:895-911.
    • (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
  • 50
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • Rothman, J.E. 1994. Mechanism of intracellular protein transport. Nature. 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 51
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman, J.E., and G. Warren. 1994. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4:220-233.
    • (1994) Curr. Biol. , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 52
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J.E., and F.T. Wieland. 1996. Protein sorting by transport vesicles. Science. 272:227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 54
    • 0021148465 scopus 로고
    • Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste, J., and E. Kuismanen. 1984. Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell. 38:535-549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 55
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste, J., and K. Svensson. 1991. Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci. 100:415-430.
    • (1991) J. Cell Sci. , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 56
    • 0023581760 scopus 로고
    • Antibodies to rat pancreas Golgi subfractions: Identification of a 58-kD cis-Golgi protein
    • Saraste, J., G.E. Palade, and M.G. Farquhar. 1987. Antibodies to rat pancreas Golgi subfractions: identification of a 58-kD cis-Golgi protein. J. Cell Biol. 105:2021-2029.
    • (1987) J. Cell Biol. , vol.105 , pp. 2021-2029
    • Saraste, J.1    Palade, G.E.2    Farquhar, M.G.3
  • 57
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science. 271:1526-1532.
    • (1996) Science , vol.271 , pp. 1526-1532
    • Schekman, R.1    Orci, L.2
  • 58
    • 0029058492 scopus 로고
    • Membrane trafficking in the presynaptic nerve terminal
    • Scheller, R.H. 1995. Membrane trafficking in the presynaptic nerve terminal. Neuron. 14:893-897.
    • (1995) Neuron. , vol.14 , pp. 893-897
    • Scheller, R.H.1
  • 59
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer, A., J.A.M. Fransen, T. Bachi, L. Ginsel, and H.-P. Hauri. 1988. Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107:1643-1653.
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.M.2    Bachi, T.3    Ginsel, L.4    Hauri, H.-P.5
  • 60
    • 0025610518 scopus 로고
    • Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus
    • Schweizer, A., J.A.M. Fransen, K. Matter, T.E. Kreis, L. Ginsel., and H.-P. Hauri. 1990. Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus. Eur. J. Cell Biol. 53:185-196.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 185-196
    • Schweizer, A.1    Fransen, J.A.M.2    Matter, K.3    Kreis, T.E.4    Ginsel, L.5    Hauri, H.-P.6
  • 61
    • 0028966452 scopus 로고
    • Human SEC13Rp functions in yeast and is localized on transport vesicles budding from the endoplasmic reticulum
    • Shaywitz, D. A., L. Orci, M. Ravazzola, A. Swaroop, and C.A. Kaiser. 1995. Human SEC13Rp functions in yeast and is localized on transport vesicles budding from the endoplasmic reticulum. J. Cell Biol. 128:769-777.
    • (1995) J. Cell Biol. , vol.128 , pp. 769-777
    • Shaywitz, D.A.1    Orci, L.2    Ravazzola, M.3    Swaroop, A.4    Kaiser, C.A.5
  • 65
    • 15844394630 scopus 로고    scopus 로고
    • GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi transport
    • Subramaniam, V.N., F. Peter, R. Philip, S.H. Wong, and W. Hong. 1996. GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi transport. Science. 272:1161-1163.
    • (1996) Science , vol.272 , pp. 1161-1163
    • Subramaniam, V.N.1    Peter, F.2    Philip, R.3    Wong, S.H.4    Hong, W.5
  • 66
    • 0030881792 scopus 로고    scopus 로고
    • NSF and α-SNAP mediate dissociation of GS28-syntaxin 5 Golgi SNARE complex
    • Subramaniam, V.N., E. Loh, and W. Hong. 1997. NSF and α-SNAP mediate dissociation of GS28-syntaxin 5 Golgi SNARE complex. J. Biol. Chem. 272: 25441-25444.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25441-25444
    • Subramaniam, V.N.1    Loh, E.2    Hong, W.3
  • 67
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T.C. 1995. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 68
    • 0027439583 scopus 로고
    • Molecular cloning, characterization, subcellular localization, and dynamics of p23, the mammalian KDEL receptor
    • Tang, B.L., SH. Wong, X.L. Qi, S.H. Low, and W. Hong. 1993. Molecular cloning, characterization, subcellular localization, and dynamics of p23, the mammalian KDEL receptor. J. Cell Biol. 120:325-338.
    • (1993) J. Cell Biol. , vol.120 , pp. 325-338
    • Tang, B.L.1    Wong, S.H.2    Qi, X.L.3    Low, S.H.4    Hong, W.5
  • 69
    • 0028823747 scopus 로고
    • Differential response of resident proteins and cycling proteins of the Golgi to brefeldin A
    • Tang, B.L., S.H. Low, and W. Hong. 1995a. Differential response of resident proteins and cycling proteins of the Golgi to brefeldin A. Eur. J. Cell Biol. 68:199-205.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 199-205
    • Tang, B.L.1    Low, S.H.2    Hong, W.3
  • 70
    • 0029557415 scopus 로고
    • Segregation of ERGIC53 and the mammalian KDEL receptor upon exit from the 15°C compartment
    • Tang, B.L., S.H. Low, H.-P. Hauri, and W. Hong. 1995b. Segregation of ERGIC53 and the mammalian KDEL receptor upon exit from the 15°C compartment. Eur. J. Cell Biol. 68:398-410.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 398-410
    • Tang, B.L.1    Low, S.H.2    Hauri, H.-P.3    Hong, W.4
  • 71
    • 0000505092 scopus 로고    scopus 로고
    • The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus
    • Tang, B.L., F. Peter, J. Krijnse-Locker, S.H. Low, G. Griffiths, and W. Hong. 1997. The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus. Mol. Cell. Biol. 17:256-266.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 256-266
    • Tang, B.L.1    Peter, F.2    Krijnse-Locker, J.3    Low, S.H.4    Griffiths, G.5    Hong, W.6
  • 72
    • 0030995064 scopus 로고    scopus 로고
    • p53/58 binds COPI and is required for selective transport through the early secretory pathway
    • Tisdale, E.J., H. Plutner, J. Matteson, and W.E. Balch. 1997. p53/58 binds COPI and is required for selective transport through the early secretory pathway. J. Cell Biol. 137:581-593.
    • (1997) J. Cell Biol. , vol.137 , pp. 581-593
    • Tisdale, E.J.1    Plutner, H.2    Matteson, J.3    Balch, W.E.4
  • 73
    • 0024432435 scopus 로고
    • The response of the Golgi complex to microtubule alternations: The role of metabolic energy and membrane traffic in Golgi complex organization
    • Turner, J.R., and A.M. Tartakoff. 1989. The response of the Golgi complex to microtubule alternations: the role of metabolic energy and membrane traffic in Golgi complex organization. J. Cell Biol. 109:2081-2088.
    • (1989) J. Cell Biol. , vol.109 , pp. 2081-2088
    • Turner, J.R.1    Tartakoff, A.M.2
  • 74
    • 0028835784 scopus 로고
    • SNAPs and NSF: General members of the fusion apparatus
    • Whiteheart, S.W., and E.W. Kubalek. 1995. SNAPs and NSF: general members of the fusion apparatus. Trends Cell Biol. 5:64-69.
    • (1995) Trends Cell Biol. , vol.5 , pp. 64-69
    • Whiteheart, S.W.1    Kubalek, E.W.2


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