Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation.
Mol Biol Cell
; 27(6): 967-78, 2016 Mar 15.
Article
em En
| MEDLINE
| ID: mdl-26823012
ABSTRACT
Small G-proteins are key regulatory molecules that activate the actin nucleation machinery to drive cytoskeletal rearrangements during plasma membrane remodeling. However, the ability of small G-proteins to interact with nucleation factors on internal membranes to control trafficking processes has not been well characterized. Here we investigated roles for members of the Rho, Arf, and Rab G-protein families in regulating WASP homologue associated with actin, membranes, and microtubules (WHAMM), an activator of Arp2/3 complex-mediated actin nucleation. We found that Rab1 stimulated the formation and elongation of WHAMM-associated membrane tubules in cells. Active Rab1 recruited WHAMM to dynamic tubulovesicular structures in fibroblasts, and an active prenylated version of Rab1 bound directly to an N-terminal domain of WHAMM in vitro. In contrast to other G-protein-nucleation factor interactions, Rab1 binding inhibited WHAMM-mediated actin assembly. This ability of Rab1 to regulate WHAMM and the Arp2/3 complex represents a distinct strategy for membrane remodeling in which a Rab G-protein recruits the actin nucleation machinery but dampens its activity.
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Base de dados:
MEDLINE
Assunto principal:
Citoesqueleto de Actina
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Membrana Celular
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Proteínas rab de Ligação ao GTP
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Complexo 2-3 de Proteínas Relacionadas à Actina
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Proteínas de Membrana
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Proteínas Associadas aos Microtúbulos
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article