Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity

FEBS Letters

Fong, Chee Wai¹  Chen, Canhe¹  Wang, Huashan¹  Lin, Sheng-Cai¹ 

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

关键词: Regulators of G-protein signaling;    G protein;    Phosphorylation;    α2A Adrenergic receptor;    Epinephrine;    RGS;    regulators of G-protein signaling;    GPCR;    G-protein-coupled receptor;    MAPK;    mitogen-activated protein kinase;    ERK;    extracellular signal-regulated protein kinase;    GAP;    GTPase-activating protein;    GAIP;    Gα-interacting protein;   

DOI  :  10.1016/S0014-5793(01)02757-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Regulators of G-protein signaling (RGS) are GTPase-activating proteins (GAP) for activated Gα subunits. We found that mouse RGS16, when expressed in HEK293T cells, is phosphorylated constitutively at serine 194 based on in vivo orthophosphate labeling experiments, while serine 53 is phosphorylated in a ligand-dependent manner upon stimulation by epinephrine in cells expressing the α2A adrenergic receptor. Phosphorylation on both sites impairs its GAP activity and subsequent attenuation on heterotrimeric G-protein-stimulated extracellular signal-regulated protein kinase activity. This is the first report of RGS functional downregulation by phosphorylation via a G-protein-coupled receptor.

【 授权许可】

Unknown