Skip to main content

Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10).

Publication ,  Journal Article
Burgon, PG; Lee, WL; Nixon, AB; Peralta, EG; Casey, PJ
Published in: J Biol Chem
August 31, 2001

Heterotrimeric G proteins are involved in the transduction of hormonal and sensory signals across plasma membranes of eukaryotic cells. Hence, they are a critical point of control for a variety of agents that modulate cellular function. Activation of these proteins is dependent on GTP binding to their alpha (Galpha) subunits. Regulators of G protein signaling (RGS) bind specifically to activated Galpha proteins, potentiating the intrinsic GTPase activity of the Galpha proteins and thus expediting the termination of Galpha signaling. Although there are several points in most G protein controlled signaling pathways that are affected by reversible covalent modification, little evidence has been shown addressing whether or not the functions of RGS proteins are themselves regulated by such modifications. We report in this study the acute functional regulation of RGS10 thru the specific and inducible phosphorylation of RGS10 protein at serine 168 by cAMP-dependent kinase A. This phosphorylation nullifies the RGS10 activity at the plasma membrane, which controls the G protein-dependent activation of the inwardly rectifying potassium channel. Surprisingly, the phosphorylation-mediated attenuation of RGS10 activity was not manifested in an alteration of its ability to accelerate GTPase activity of Galpha. Rather, the phosphorylation event correlates with translocation of RGS10 from the plasma membrane and cytosol into the nucleus.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

August 31, 2001

Volume

276

Issue

35

Start / End Page

32828 / 32834

Location

United States

Related Subject Headings

  • Xenopus laevis
  • Transfection
  • Serine
  • Recombinant Proteins
  • Receptors, Muscarinic
  • Receptor, Muscarinic M2
  • RGS Proteins
  • Protein Transport
  • Potassium Channels, Inwardly Rectifying
  • Potassium Channels
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Burgon, P. G., Lee, W. L., Nixon, A. B., Peralta, E. G., & Casey, P. J. (2001). Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10). J Biol Chem, 276(35), 32828–32834. https://doi.org/10.1074/jbc.M100960200
Burgon, P. G., W. L. Lee, A. B. Nixon, E. G. Peralta, and P. J. Casey. “Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10).J Biol Chem 276, no. 35 (August 31, 2001): 32828–34. https://doi.org/10.1074/jbc.M100960200.
Burgon PG, Lee WL, Nixon AB, Peralta EG, Casey PJ. Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10). J Biol Chem. 2001 Aug 31;276(35):32828–34.
Burgon, P. G., et al. “Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10).J Biol Chem, vol. 276, no. 35, Aug. 2001, pp. 32828–34. Pubmed, doi:10.1074/jbc.M100960200.
Burgon PG, Lee WL, Nixon AB, Peralta EG, Casey PJ. Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10). J Biol Chem. 2001 Aug 31;276(35):32828–32834.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

August 31, 2001

Volume

276

Issue

35

Start / End Page

32828 / 32834

Location

United States

Related Subject Headings

  • Xenopus laevis
  • Transfection
  • Serine
  • Recombinant Proteins
  • Receptors, Muscarinic
  • Receptor, Muscarinic M2
  • RGS Proteins
  • Protein Transport
  • Potassium Channels, Inwardly Rectifying
  • Potassium Channels