The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro
AUTOR(ES)
Popov, Serguei
FONTE
The National Academy of Sciences of the USA
RESUMO
Regulators of G protein signaling (RGS) proteins accelerate GTP hydrolysis by Gi but not by Gs class α-subunits. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. We have demonstrated that the RGS domains of RGS4, RGS10, and GAIP retain GTPase accelerating activity with the Gi class substrates Giα1, Goα, and Gzα in vitro. No regulatory activity of the RGS domains was detected for Gsα. Short deletions within the RGS domain of RGS4 destroyed GTPase activating protein activity and Giα1 substrate binding. Comparable protein–protein interactions between Giα1–GDP–AlF4− and the RGS domain or full-length RGS4 were detected using surface plasmon resonance.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=23796Documentos Relacionados
- Clathrin-coated vesicles bearing GAIP possess GTPase-activating protein activity in vitro
- RGS-GAIP, a GTPase-activating Protein for Gαi Heterotrimeric G Proteins, Is Located on Clathrin-coated Vesicles
- RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα
- Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells
- Fidelity of G protein β-subunit association by the G protein γ-subunit-like domains of RGS6, RGS7, and RGS11