Second messengers regulate RGS2 expression which is targeted to the nucleus

Jaroslaw W. Zmijewski, Ling Song, Lualhati Harkins, Charles S. Cobbs, Richard S. Jope

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


Regulators of G-protein Signaling (RGS) proteins attenuate signaling activities of G proteins, and modulation of expression appears to be a primary mechanism for regulating RGS proteins. In human astrocytoma 1321N1 cells RGS2 expression was increased by activation of muscarinic receptors coupled to phosphoinositide signaling with carbachol, or by increased cyclic AMP production, demonstrating that both signaling systems can increase the expression of a RGS family member in a single cell type. Carbachol-stimulated increases in endogenous RGS2 protein levels appeared by immunocytochemical analysis to be largely confined to the nucleus, and this localization was confirmed by Western blot analysis which showed increased nuclear, but not cytosolic, RGS2 after carbachol treatment. Additionally, transiently expressed green fluorescent protein (GFP)-tagged, 6×His-tagged, or unmodified RGS2 resulted in a predominant nuclear localization, as well as a distinct accumulation of RGS2 along the plasma membrane. The intranuclear localization of GFP-RGS2 was confirmed with confocal microscopy. Thus, RGS2 expression is rapidly and transiently increased by phosphoinositide signaling and by cyclic AMP, and endogenous and transfected RGS2 is largely, although not entirely, localized in the nucleus.

Original languageEnglish (US)
Pages (from-to)201-211
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number3
StatePublished - Dec 19 2001
Externally publishedYes


  • Cyclic AMP
  • G protein
  • Phosphoinositide signaling
  • Regulator of G protein signaling
  • RGS2

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Biophysics


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