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Translational control by RGS2.


ABSTRACT: The regulator of G protein signaling (RGS) proteins are a family of guanosine triphosphatase (GTPase)-accelerating proteins. We have discovered a novel function for RGS2 in the control of protein synthesis. RGS2 was found to bind to eIF2Bepsilon (eukaryotic initiation factor 2B epsilon subunit) and inhibit the translation of messenger RNA (mRNA) into new protein. This effect was not observed for other RGS proteins tested. This novel function of RGS2 is distinct from its ability to regulate G protein-mediated signals and maps to a stretch of 37 amino acid residues within its conserved RGS domain. Moreover, RGS2 was capable of interfering with the eIF2-eIF2B GTPase cycle, which is a requisite step for the initiation of mRNA translation. Collectively, this study has identified a novel role for RGS2 in the control of protein synthesis that is independent of its established RGS domain function.

SUBMITTER: Nguyen CH 

PROVIDER: S-EPMC2742185 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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Translational control by RGS2.

Nguyen Chau H CH   Ming Hong H   Zhao Peishen P   Hugendubler Lynne L   Gros Robert R   Kimball Scot R SR   Chidiac Peter P  

The Journal of cell biology 20090901 5


The regulator of G protein signaling (RGS) proteins are a family of guanosine triphosphatase (GTPase)-accelerating proteins. We have discovered a novel function for RGS2 in the control of protein synthesis. RGS2 was found to bind to eIF2Bepsilon (eukaryotic initiation factor 2B epsilon subunit) and inhibit the translation of messenger RNA (mRNA) into new protein. This effect was not observed for other RGS proteins tested. This novel function of RGS2 is distinct from its ability to regulate G pro  ...[more]

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