Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A.

ABSTRACT: RGS (regulators of G-protein signalling) modulate signalling by acting as GAPs (GTPase-activating proteins) for alpha subunits of heterotrimeric G-proteins. RGS14 accelerates GTP hydrolysis by G(ialpha) family members through its RGS domain and suppresses guanine nucleotide dissociation from G(ialpha1) and G(ialpha3) subunits through its C-terminal GoLoco domain. Additionally, RGS14 binds the activated forms of the small GTPases Rap1 and Rap2 by virtue of tandem RBDs (Raf-like Ras/Rap binding domains). RGS14 was identified in a screen for Rap2 effectors [Traver, Splingard, Gaudriault and De Gunzburg (2004) Biochem. J. 379, 627-632]. In the present study, we tested whether Rap binding regulates RGS14's biochemical activities. We found that RGS14 activity towards heterotrimeric G-proteins, a

SUBMITTER: Mittal V 

PROVIDER: S-EPMC1386029 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature