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Article Dans Une Revue Biochemical Journal Année : 2008

A BAR domain-mediated autoinhibitory mechanism for RhoGAPs of the GRAF family

Alexander Eberth
  • Fonction : Auteur
Richard Lundmark
  • Fonction : Auteur
Lothar Gremer
Radovan Dvorsky
  • Fonction : Auteur
Katja T Koessmeier
  • Fonction : Auteur
Harvey T Mcmahon
  • Fonction : Auteur

Résumé

The BAR (Bin-Amphiphysin-Rvs) domain defines an emerging superfamily of proteins implicated in fundamental biological processes by sensing and inducing membrane curvature. We identified a novel autoregulatory function for the BAR domain of two related GTPase activating proteins (GAPs) of the GRAF subfamily. We demonstrate that the N-terminal fragment of these GAPs including the BAR domain interacts directly with the GAP domain and inhibits its activity. Analysis of various BAR- and GAP domains revealed that the BAR domain-mediated inhibition of these GAPs function is highly specific. These GAPs, in their autoinhibited state, are able to bind and tubulate liposomes in vitro, and to generate lipid tubules in cells. Taken together, we identified BAR domains as cis-acting inhibitory elements that very likely mask the active sites of the GAP domains and thus prevent downregulation of Rho proteins. Most remarkably, these BAR proteins represent a dual-site system with separate membrane tubulation and GAP inhibitory functions that operate simultaneously.

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Dates et versions

hal-00479075 , version 1 (30-04-2010)

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Alexander Eberth, Richard Lundmark, Lothar Gremer, Radovan Dvorsky, Katja T Koessmeier, et al.. A BAR domain-mediated autoinhibitory mechanism for RhoGAPs of the GRAF family. Biochemical Journal, 2008, 417 (1), pp.371-377. ⟨10.1042/BJ20081535⟩. ⟨hal-00479075⟩

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