Format

Send to

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 2001 Aug 24;504(1-2):16-22.

Multiple phosphorylation sites in RGS16 differentially modulate its GAP activity.

Author information

  • 1Regulatory Biology Group, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Singapore.

Abstract

Regulators of G-protein signaling (RGS) are GTPase-activating proteins (GAP) for activated Galpha 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 alpha2A 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.

PMID:
11522288
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Support Center