A novel phosphorylation-dependent RNase activity of GAP-SH3 binding protein: A potential link between signal transduction and RNA stability

Imed Eddine Gallouzi, Fabienne Parker, Karim Chebli, Florence Maurier, Emmanuel Labourier, Isabelle Barlat, Jean Paul Capony, Bruno Tocque, Jamal Tazi

Research output: Contribution to journalArticle

146 Citations (Scopus)

Abstract

A potential p120 GTPase-activating protein (RasGAP) effector, G3BP (RasGAP Src homology 3 [SH3] binding protein), was previously identified based on its ability to bind the SH3 domain of RasGAP. Here er show that G3BP colocalizes and physically interacts with RasGAP at the plasma membrane of serum-stimulated but not quiescent Chinese hamster lung fibroblasts. In quiescent cells, G3BP was hyperphosphorylated on serine residues, and this modification was essential for its activity. Indeed, G3BP harbors a phosphorylation-dependent RNase activity which specifically cleaves the 3'- untranslated region of human c-myc mRNA. The endoribonuclease activity of G3BP can initiate mRNA degradation and therefore represents a link between a RasGAP-mediated signaling pathway and RNA turnover.

Original languageEnglish
Pages (from-to)3956-3965
Number of pages10
JournalMolecular and Cellular Biology
Volume18
Issue number7
DOIs
Publication statusPublished - Jul 1998

    Fingerprint

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this