RGS2 is a component of the cellular stress response

Chau H. Nguyen, Peishen Zhao, Alina J. Sobiesiak, Peter Chidiac

Research output: Contribution to journalArticleResearchpeer-review

8 Citations (Scopus)

Abstract

Regulator of G protein signaling (RGS) proteins are GTPase accelerating proteins for heterotrimeric G protein α-subunits. RGS2 has recently been shown to have additional G protein-independent functions including control of ion channel currents, microtubule polymerization, and protein synthesis. Cellular levels of RGS2 mRNA and protein are upregulated in response to various forms of stress suggesting that it may be a stress-adaptive protein; however, direct evidence to support this notion has remained elusive. In this report, we show that thermal stress upregulates RGS2 expression and this serves to arrest de novo protein synthesis. The latter is an established cellular response to stress. Inhibiting the stress-induced RGS2 upregulation by way of siRNA knockdown diminished the repression of global protein synthesis. The collective results of our study implicate RGS2 upregulation as a cellular mechanism of controlling de novo protein synthesis in response to stress. This work provides greater insight into the stress proteome and the role of RGS2.

Original languageEnglish
Pages (from-to)129-134
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume426
Issue number1
DOIs
Publication statusPublished - 14 Sep 2012
Externally publishedYes

Keywords

  • Cellular stress response
  • Protein synthesis
  • RGS protein
  • Translation

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