The core domain of RGS16 retains G‐protein binding and GAP activity in vitro, but is not functional in vivo

FEBS Letters

Chen, Canhe¹  Lin, Sheng-Cai¹ 

[1] Regulatory Biology Laboratory, Institute of Molecular and Cell Biology, National University of Singapore, 30 Medical Drive, Singapore 117609, Singapore

关键词: RGS protein;    RGS16;    GTP-binding protein;    GTPase-activating protein;    RGS;    regulator of G-protein signaling;    GAP;    GTPase-activating protein;    G-protein;    GTP-binding protein;    GST;    glutathione S-transferase;    PKA;    protein kinase A;   

DOI  :  10.1016/S0014-5793(98)00042-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The regulators of G-protein signaling (RGS) family members contain a conserved region, the RGS domain, and are GTPase-activating proteins for many members of G-protein α-subunits. We report here that the core domain of RGS16 is sufficient for in vitro biochemical functions as assayed by its G-protein binding affinity and its ability to stimulate GTP hydrolysis by Gα_o protein. RGS16 also requires, in addition to the RGS domain, the divergent N-terminus for its biological function in the attenuation of pheromone signaling in yeast, whereas its C-terminus region is dispensable. Together with other evidence, these data support the notion that RGS proteins interact with other cellular factors and may serve to link specific G-proteins to different downstream effectors in G-protein-mediated signaling pathways.

【 授权许可】

Unknown