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Volumn 78, Issue 5, 1999, Pages 305-310

The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval

Author keywords

ARF; COPI; Endoplasmic reticulum; GAP; Golgi

Indexed keywords

GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; ZINC FINGER PROTEIN;

EID: 0033029458     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0171-9335(99)80064-8     Document Type: Article
Times cited : (39)

References (31)
  • 2
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeast by electroporation
    • Becker, D. M., L. Guarente: High-efficiency transformation of yeast by electroporation. Methods Enzymol. 194, 182-187 (1991).
    • (1991) Methods Enzymol. , vol.194 , pp. 182-187
    • Becker, D.M.1    Guarente, L.2
  • 3
    • 0028904466 scopus 로고
    • Arf proteins: The membrane traffic police?
    • Boman, A. L., R. A. Kahn: Arf proteins: the membrane traffic police? Trends Biochem. Sci. 20, 147-150 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 147-150
    • Boman, A.L.1    Kahn, R.A.2
  • 4
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson, P., F. Letourneur: Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629-1631 (1994).
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 5
    • 0029988456 scopus 로고    scopus 로고
    • Delta- und zeta-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval
    • Cosson, P., C. Démollière, S. Hennecke, R. Duden, F. Letourneur: Delta- und zeta-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval. EMBO J. 15, 1792-1798 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1792-1798
    • Cosson, P.1    Démollière, C.2    Hennecke, S.3    Duden, R.4    Letourneur, F.5
  • 6
    • 0029416828 scopus 로고
    • The ARF1 GTPase-activating protein: Zinc finger motif and Golgi complex localization
    • Cukierman, E., I. Huber, M. Rotman, D. Cassel: The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science 270, 1999-2002 (1995).
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 7
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes
    • Donaldson, J. G., D. Cassel, R. A. Kahn, R. D. Klausner: ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA 89, 6408-6412 (1992).
    • (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
  • 8
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler, K., M. Veit, M. A. Stammes, J. E. Rothman: Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 273, 1396-1399 (1996).
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stammes, M.A.3    Rothman, J.E.4
  • 9
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor, E. C., S. T. Heesen, T. R. Graham, M. Aebi, S. D. Emr: Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J. Cell Biol. 127, 636-647 (1994).
    • (1994) J. Cell Biol. , vol.127 , pp. 636-647
    • Gaynor, E.C.1    Heesen, S.T.2    Graham, T.R.3    Aebi, M.4    Emr, S.D.5
  • 10
    • 0031027758 scopus 로고    scopus 로고
    • COPI-independent anterograde transport: Cargo-selective ER to Golgi protein transport in yeast COPI mutants
    • Gaynor, E. C., S. D. Emr: COPI-independent anterograde transport: cargo-selective ER to Golgi protein transport in yeast COPI mutants. J. Cell Biol. 136, 789-802 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 789-802
    • Gaynor, E.C.1    Emr, S.D.2
  • 11
    • 0031940702 scopus 로고    scopus 로고
    • ARF is required for maintenance of yeast Golgi and endosome structure and function
    • Gaynor, E. C., C. Y. Chen, S. D. Emr, T. R. Graham: ARF is required for maintenance of yeast Golgi and endosome structure and function. Mol. Biol. Cell 9, 653-670 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 653-670
    • Gaynor, E.C.1    Chen, C.Y.2    Emr, S.D.3    Graham, T.R.4
  • 12
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., A. Sugino: New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74, 527-534 (1988).
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 13
    • 0032544657 scopus 로고    scopus 로고
    • Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein
    • Huber, I., E. Cukierman, M. Rotman, T. Aoe, V. W. Hsu, D. Cassel: Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein. J. Biol. Chem. 273, 24786-24791 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 24786-24791
    • Huber, I.1    Cukierman, E.2    Rotman, M.3    Aoe, T.4    Hsu, V.W.5    Cassel, D.6
  • 14
    • 0028017275 scopus 로고
    • A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation
    • Ireland, L. S., G. C. Johnston, M. A. Drebot, N. Dhillon, A. J. De Maggio, M. F. Hoekstra, R. A. Singer: A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation. EMBO J. 13, 3812-3821 (1994).
    • (1994) EMBO J. , vol.13 , pp. 3812-3821
    • Ireland, L.S.1    Johnston, G.C.2    Drebot, M.A.3    Dhillon, N.4    De Maggio, A.J.5    Hoekstra, M.F.6    Singer, R.A.7
  • 15
    • 0026073301 scopus 로고
    • Classical Mutagenesis techniques
    • Lawrence, C. W.: Classical Mutagenesis techniques. Methods Enzymol. 194, 273-281 (1991).
    • (1991) Methods Enzymol. , vol.194 , pp. 273-281
    • Lawrence, C.W.1
  • 19
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer, D. J., J. B. Helms, C. J. Beckers, L. Orci, J. E. Rothman: Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J. Biol. Chem. 268, 12083-12089 (1993).
    • (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
  • 21
    • 0033081078 scopus 로고    scopus 로고
    • Retrograde transport from the yeast Golgi is mediated by two ARF-GAP proteins with overlapping function
    • Poon, P. P., D. Cassel, A. Spang, M. Rotman, E. Pick, R. A. Singer, G. C. Johnston: Retrograde transport from the yeast Golgi is mediated by two ARF-GAP proteins with overlapping function. EMBO J. 18, 555-564 (1999).
    • (1999) EMBO J. , vol.18 , pp. 555-564
    • Poon, P.P.1    Cassel, D.2    Spang, A.3    Rotman, M.4    Pick, E.5    Singer, R.A.6    Johnston, G.C.7
  • 22
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J. E., L. Orci: Molecular dissection of the secretory pathway. Nature 355, 409-415 (1992).
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 23
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J. E., F. T. Wieland: Protein sorting by transport vesicles. Science 272, 227-234 (1996).
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 24
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., L. Orci: Coat proteins and vesicle budding. Science 271, 1526-1532 (1996).
    • (1996) Science , vol.271 , pp. 1526-1532
    • Schekman, R.1    Orci, L.2
  • 25
    • 0025978950 scopus 로고
    • Micromanipulation and dissection of asci
    • Sherman, F., J. Hicks: Micromanipulation and dissection of asci. Methods Enzymol. 194, 21-37 (1991).
    • (1991) Methods Enzymol. , vol.194 , pp. 21-37
    • Sherman, F.1    Hicks, J.2
  • 26
    • 0025174078 scopus 로고
    • ADP-ribosylation factor is functionally and physically associated with the Golgi complex
    • Stearns, T., M. C. Willingham, D. Botstein, R. A. Kahn: ADP-ribosylation factor is functionally and physically associated with the Golgi complex. Proc. Natl. Acad. Sci. USA 87, 1238-1242 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1238-1242
    • Stearns, T.1    Willingham, M.C.2    Botstein, D.3    Kahn, R.A.4
  • 27
    • 0027724473 scopus 로고
    • Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles
    • Tanigawa, G., L. Orci, M. Amherdt, M. Ravazzola, J. B. Helms, J. E. Rothman: Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J. Cell Biol. 123, 1365-1371 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 1365-1371
    • Tanigawa, G.1    Orci, L.2    Amherdt, M.3    Ravazzola, M.4    Helms, J.B.5    Rothman, J.E.6
  • 28
    • 0028124181 scopus 로고
    • An activating mutation in ARF1 stabilizes coatomer binding to Golgi membranes
    • Teal, S. B., V. W. Hsu, P. J. Peters, R. D. Klausner, J. G. Donaldson: An activating mutation in ARF1 stabilizes coatomer binding to Golgi membranes. J. Biol. Chem. 269, 3135-3138 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 3135-3138
    • Teal, S.B.1    Hsu, V.W.2    Peters, P.J.3    Klausner, R.D.4    Donaldson, J.G.5
  • 29
    • 0027510252 scopus 로고
    • Yeast Wbp1p and Swp1p form a protein complex essential for oligosaccharyltransferase activity
    • te Heesen, S., R. Knauer, L. Lehle, M. Aebi: Yeast Wbp1p and Swp1p form a protein complex essential for oligosaccharyltransferase activity. EMBO J. 12, 279-284 (1993).
    • (1993) EMBO J. , vol.12 , pp. 279-284
    • Te Heesen, S.1    Knauer, R.2    Lehle, L.3    Aebi, M.4
  • 31
    • 0032584676 scopus 로고    scopus 로고
    • A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae
    • Zhang, C. J., M. M. Cavenagh, R. A. Kahn: A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 273, 19792-19796 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 19792-19796
    • Zhang, C.J.1    Cavenagh, M.M.2    Kahn, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.