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Article Dans Une Revue Journal of Biological Chemistry Année : 2004

Phospholipids can switch the GTPase substrate preference of a GTPase-activating protein.

Erzsébet Ligeti
  • Fonction : Auteur
  • PersonId : 941028
Samuel E Hernandez
  • Fonction : Auteur
Anthony J Koleske
  • Fonction : Auteur
Jeffrey Settleman
  • Fonction : Auteur
  • PersonId : 941029

Résumé

The major cellular inhibitors of the small GTPases of the Ras superfamily are the GTPase-activating proteins (GAPs), which stimulate the intrinsic GTP hydrolyzing activity of GTPases, thereby inactivating them. The catalytic activity of several GAPs is reportedly inhibited or stimulated by various phospholipids and fatty acids in vitro, indicating a likely physiological role for lipids in regulating small GTPases. We find that the p190 RhoGAP, a potent GAP for the Rho and Rac GTPases, is similarly sensitive to phospholipids. Interestingly, however, several of the tested phospholipids were found to effectively inhibit the RhoGAP activity of p190 but stimulate its RacGAP activity. Thus, phospholipids have the ability to "switch" the GTPase substrate preference of a GAP, thereby providing a novel regulatory mechanism for the small GTPases.

Domaines

Immunité innée

Dates et versions

hal-00820747 , version 1 (06-05-2013)

Identifiants

Citer

Erzsébet Ligeti, Marie-Claire Dagher, Samuel E Hernandez, Anthony J Koleske, Jeffrey Settleman. Phospholipids can switch the GTPase substrate preference of a GTPase-activating protein.. Journal of Biological Chemistry, 2004, 279 (7), pp.5055-8. ⟨10.1074/jbc.C300547200⟩. ⟨hal-00820747⟩

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