메뉴 건너뛰기




Volumn 405, Issue 6788, 2000, Pages 800-804

The γ-subunit of the coatomer complex binds Cdc42 to mediate transformation

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATE; MUTANT PROTEIN; PROTEIN SUBUNIT;

EID: 0001264854     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35015585     Document Type: Article
Times cited : (188)

References (30)
  • 1
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D. G. & Nelson, W. J. Origins of cell polarity. Cell 84, 335-344 (1996).
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 2
    • 0033007293 scopus 로고    scopus 로고
    • Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity
    • Johnson, D. I. Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol. Mol. Biol. Rev. 63, 54-105 (1999).
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 54-105
    • Johnson, D.I.1
  • 3
    • 0031260578 scopus 로고    scopus 로고
    • A novel Cdc42Hs mutant induces cellular transformation
    • Lin, R., Bagrodia, S., Cerione, R. A. & Manor, D. A novel Cdc42Hs mutant induces cellular transformation. Curr. Biol. 7, 794-797 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 794-797
    • Lin, R.1    Bagrodia, S.2    Cerione, R.A.3    Manor, D.4
  • 4
    • 0026044409 scopus 로고
    • Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product
    • Hart, M. J., Eva, A., Evans, T., Aaronson, S. A. & Cerione, R. A. Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product. Nature 354, 311-314 (1991).
    • (1991) Nature , vol.354 , pp. 311-314
    • Hart, M.J.1    Eva, A.2    Evans, T.3    Aaronson, S.A.4    Cerione, R.A.5
  • 5
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Racl
    • Manser, E., Leung, T., Salihuddin, H., Zhao, Z.-S. & Lim, L. A brain serine/threonine protein kinase activated by Cdc42 and Racl. Nature 367, 40-46 (1994).
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.-S.4    Lim, L.5
  • 7
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPas CDC42Hs, is implicated inactin polymerization
    • Symons, M. et al. Wiskott-Aldrich syndrome protein, a novel effector for the GTPas CDC42Hs, is implicated inactin polymerization. Cell 84, 723-734 (1996).
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1
  • 8
    • 0029891491 scopus 로고    scopus 로고
    • IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs
    • Hart, M. J., Callow, M. G., Souza, B. & Polakis, P. IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs. EMBO J. 15, 2997-3005 (1996).
    • (1996) EMBO J. , vol.15 , pp. 2997-3005
    • Hart, M.J.1    Callow, M.G.2    Souza, B.3    Polakis, P.4
  • 9
    • 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. et al. 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, 239-253 (1991).
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1
  • 10
    • 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, 248-251 (1991).
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.G.1    Serafini, T.2    Rothman, J.E.3
  • 11
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. Mechanisms of intracellular protein transport. Nature 372, 55-63 (1994).
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 12
    • 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. et al. 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, 1902-1906 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1902-1906
    • Harter, C.1
  • 13
    • 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, 31364-31371 (1995).
    • (1995) J. Biol., Chem. , vol.270 , pp. 31364-31371
    • Lowe, M.1    Kreis, T.E.2
  • 14
    • 0028643562 scopus 로고
    • Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum
    • Letourner, F. et al. Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell 79, 1199-1207 (1994).
    • (1994) Cell , vol.79 , pp. 1199-1207
    • Letourner, F.1
  • 15
    • 0032578522 scopus 로고    scopus 로고
    • A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer
    • Harter, C. & Wieland, F. T. A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer. Proc. Natl Acad. Sci. USA 95, 11649-11654 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11649-11654
    • Harter, C.1    Wieland, F.T.2
  • 16
    • 0033582648 scopus 로고    scopus 로고
    • Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors
    • Bremser, M. et al. Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. Cell 96, 495-506 (1999).
    • (1999) Cell , vol.96 , pp. 495-506
    • Bremser, M.1
  • 17
    • 0030859462 scopus 로고    scopus 로고
    • Identification of an actin cytoskeletal complex that includes IQGAP and the Cdc42 GTPase
    • Erickson, J. W., Cerione, R. A. & Hart, M. J. Identification of an actin cytoskeletal complex that includes IQGAP and the Cdc42 GTPase. J. Biol. Chem. 272, 24443-24447 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 24443-24447
    • Erickson, J.W.1    Cerione, R.A.2    Hart, M.J.3
  • 18
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis, T. Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J. 5, 931-941 (1986).
    • (1986) EMBO J. , vol.5 , pp. 931-941
    • Kreis, T.1
  • 19
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • Musch, A., Xu, H., Shields, D. & Rodriguez-Boulan, E. Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells. J. Cell Biol. 133, 543-558 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 543-558
    • Musch, A.1    Xu, H.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 20
    • 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, 1437-1448 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 21
    • 0000153275 scopus 로고    scopus 로고
    • Transformation activity of Cdc42 requires a region unique to Rho-related proteins
    • Wu, W., Lin, R., Cerione, R. A. & Manor, D. Transformation activity of Cdc42 requires a region unique to Rho-related proteins. J. Biol. Chem. 273, 16655-16658 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 16655-16658
    • Wu, W.1    Lin, R.2    Cerione, R.A.3    Manor, D.4
  • 22
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski, R., Hall, A. & Mellman, I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nature Cell Biol. 1, 8-13 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 23
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus
    • Erickson, J. W., Zhang, C. J., Kahn, R. A., Evans, T. & Cerione, R. A. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J. Biol. Chem. 271, 26850-26854 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 26850-26854
    • Erickson, J.W.1    Zhang, C.J.2    Kahn, R.A.3    Evans, T.4    Cerione, R.A.5
  • 24
    • 0033551698 scopus 로고    scopus 로고
    • Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation
    • Lin, R., Cerione, R. A. & Manor, D. Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation. J. Biol. Chem. 274, 23633-23641 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 23633-23641
    • Lin, R.1    Cerione, R.A.2    Manor, D.3
  • 25
    • 0028286028 scopus 로고
    • Disruption of the Golgi apparatus by brefeldin A blocks cell polarization and inhibits directed cell migration
    • Bershadsky, A. D. & Futerman, A. H. Disruption of the Golgi apparatus by brefeldin A blocks cell polarization and inhibits directed cell migration. Proc. Natl Acad. Sci. USA 91, 5686-5689 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5686-5689
    • Bershadsky, A.D.1    Futerman, A.H.2
  • 26
    • 0029819793 scopus 로고    scopus 로고
    • Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts
    • Peranen, J., Auvinen, P., Virta, H., Wepf, R. & Simons, K. Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts. J. Cell Biol 135, 153-167 (1996).
    • (1996) J. Cell Biol , vol.135 , pp. 153-167
    • Peranen, J.1    Auvinen, P.2    Virta, H.3    Wepf, R.4    Simons, K.5
  • 27
    • 0028948382 scopus 로고
    • Multiple Ras functions can contribute to mammalian cell transformation
    • White, M. A. et al. Multiple Ras functions can contribute to mammalian cell transformation. Cell 80, 533-541 (1993).
    • (1993) Cell , vol.80 , pp. 533-541
    • White, M.A.1
  • 28
    • 0031026132 scopus 로고    scopus 로고
    • Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways
    • Westwick, J. K. et al. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol. 17, 1324-1335 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1324-1335
    • Westwick, J.K.1
  • 29
    • 0032575652 scopus 로고    scopus 로고
    • Characterization of the association of the actin-binding protein, IQGAP, and activated Cdc42 with Golgi membranes
    • McCallum, S. J., Erickson, J. W. & Cerione, R. A. Characterization of the association of the actin-binding protein, IQGAP, and activated Cdc42 with Golgi membranes. J. Biol. Chem. 273, 22537-22544 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22537-22544
    • McCallum, S.J.1    Erickson, J.W.2    Cerione, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.