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

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 we 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.

journal_name

Mol Cell Biol

authors

Gallouzi IE,Parker F,Chebli K,Maurier F,Labourier E,Barlat I,Capony JP,Tocque B,Tazi J

doi

10.1128/mcb.18.7.3956

subject

Has Abstract

pub_date

1998-07-01 00:00:00

pages

3956-65

issue

7

eissn

0270-7306

issn

1098-5549

journal_volume

18

pub_type

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