Une nouvelle protéine RhoGAP impliquée dans la régulation du complexe Arp2/3 au niveau de l’appareil de Golgi : Un relais entre les protéines G ARF1 et Cdc42

Thierry Dubois; Philippe Chavrier

doi:10.1051/medsci/2005218-9692

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Volume 21 / Numéro 8-9 (Août–Septembre 2005)

Med Sci (Paris), 21 8-9 (2005) 692-694

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Numéro		Med Sci (Paris) Volume 21, Numéro 8-9, Août–Septembre 2005


Page(s)		692 - 694
Section		Nouvelles
DOI		https://doi.org/10.1051/medsci/2005218-9692
Publié en ligne		15 août 2005

Chavrier P, Goud B. The role of ARF and rab GTPases in membrane transport. Curr Opin Cell Biol 1999; 11 : 466–75. [Google Scholar]
Donaldson JG, Jackson CL. Regulators and effectors of the ARF GTPases. Curr Opin Cell Biol 2000; 12 : 475–82. [Google Scholar]
Antonny B. Contrôle de l’assemblage des manteaux protéiques COPI par les petites protéines G Arf et Sar. Med Sci (Paris) 2002; 18 : 1012–6. [Google Scholar]
Bonifacino JS, Lippincott-Schwartz J. Coat proteins: shaping membrane transport. Nat Rev Mol Cell Biol 2003; 4 : 409–14. [Google Scholar]
Stamnes M. Regulating the actin cytoskeleton during vesicular transport. Curr Opin Cell Biol 2002; 14 : 428–33. [Google Scholar]
Carreno S, Engqvist-Goldstein AE, Zhang CX, et al. Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network. J Cell Biol 2004; 165 : 781–8. [Google Scholar]
Etienne-Manneville S, Hall A. Rho GTPases in cell biology. Nature 2002; 420 : 629–35. [Google Scholar]
Qualmann B, Mellor H. Regulation of endocytic traffic by Rho GTPases. Biochem J 2003; 371 : 233–41. [Google Scholar]
Camera P, Da Silva JS, Griffiths G, et al. Citron-N is a neuronal Rho-associated protein involved in Golgi organization through actin cytoskeleton regulation. Nat Cell Biol 2003; 5 : 1071–8. [Google Scholar]
Musch A, Cohen D, Kreitzer G, Rodriguez-Boulan E. Cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J 2001; 20 : 2171–9. [Google Scholar]
Luna A, Matas OB, Martinez-Menarguez JA, et al. Regulation of protein transport from the Golgi complex to the endoplasmic reticulum by CDC42 and N-WASP. Mol Biol Cell 2002; 13 : 866–79. [Google Scholar]
Matas OB, Martinez-Menarguez JA, Egea G. Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes. Traffic 2004; 5 : 838–46. [Google Scholar]
Wu WJ, Erickson JW, Lin R, Cerione RA. The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 2000; 405 : 800–4. [Google Scholar]
Chen JL, Lacomis L, Erdjument-Bromage H, et al. Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes. FEBS Lett 2004; 566 : 281–6. [Google Scholar]
Dubois T, Paleotti O, Mironov AA, et al. Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. Nat Cell Biol 2005; 7 : 353–64. [Google Scholar]
Basseres DS, Tizzei EV, Duarte AA, et al. ARHGAP10, a novel human gene coding for a potentially cytoskeletal Rho-GTPase activating protein. Biochem Biophys Res Commun 2002; 294 : 579–85. [Google Scholar]
Bernards A. GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim Biophys Acta 2003; 1603 : 47–82. [Google Scholar]

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[1] Chavrier P, Goud B. The role of ARF and rab GTPases in membrane transport. Curr Opin Cell Biol 1999; 11 : 466–75. [Google Scholar]

[2] Donaldson JG, Jackson CL. Regulators and effectors of the ARF GTPases. Curr Opin Cell Biol 2000; 12 : 475–82. [Google Scholar]

[3] Antonny B. Contrôle de l’assemblage des manteaux protéiques COPI par les petites protéines G Arf et Sar. Med Sci (Paris) 2002; 18 : 1012–6. [Google Scholar]

[4] Bonifacino JS, Lippincott-Schwartz J. Coat proteins: shaping membrane transport. Nat Rev Mol Cell Biol 2003; 4 : 409–14. [Google Scholar]

[5] Stamnes M. Regulating the actin cytoskeleton during vesicular transport. Curr Opin Cell Biol 2002; 14 : 428–33. [Google Scholar]

[6] Carreno S, Engqvist-Goldstein AE, Zhang CX, et al. Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network. J Cell Biol 2004; 165 : 781–8. [Google Scholar]

[7] Etienne-Manneville S, Hall A. Rho GTPases in cell biology. Nature 2002; 420 : 629–35. [Google Scholar]

[8] Qualmann B, Mellor H. Regulation of endocytic traffic by Rho GTPases. Biochem J 2003; 371 : 233–41. [Google Scholar]

[9] Camera P, Da Silva JS, Griffiths G, et al. Citron-N is a neuronal Rho-associated protein involved in Golgi organization through actin cytoskeleton regulation. Nat Cell Biol 2003; 5 : 1071–8. [Google Scholar]

[10] Musch A, Cohen D, Kreitzer G, Rodriguez-Boulan E. Cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J 2001; 20 : 2171–9. [Google Scholar]

[11] Luna A, Matas OB, Martinez-Menarguez JA, et al. Regulation of protein transport from the Golgi complex to the endoplasmic reticulum by CDC42 and N-WASP. Mol Biol Cell 2002; 13 : 866–79. [Google Scholar]

[12] Matas OB, Martinez-Menarguez JA, Egea G. Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes. Traffic 2004; 5 : 838–46. [Google Scholar]

[13] Wu WJ, Erickson JW, Lin R, Cerione RA. The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 2000; 405 : 800–4. [Google Scholar]

[14] Chen JL, Lacomis L, Erdjument-Bromage H, et al. Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes. FEBS Lett 2004; 566 : 281–6. [Google Scholar]

[15] Dubois T, Paleotti O, Mironov AA, et al. Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. Nat Cell Biol 2005; 7 : 353–64. [Google Scholar]

[16] Basseres DS, Tizzei EV, Duarte AA, et al. ARHGAP10, a novel human gene coding for a potentially cytoskeletal Rho-GTPase activating protein. Biochem Biophys Res Commun 2002; 294 : 579–85. [Google Scholar]

[17] Bernards A. GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim Biophys Acta 2003; 1603 : 47–82. [Google Scholar]