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Molecular and Cellular Biology, November 2001, p. 7747-7760, Vol. 21, No. 22
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.22.7747-7760.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

RasGAP-Associated Endoribonuclease G3BP: Selective RNA Degradation and Phosphorylation-Dependent Localization

Hélène Tourrière,1 Imed-eddine Gallouzi,2 Karim Chebli,1 Jean Paul Capony,3 John Mouaikel,1 Peter van der Geer,4 and Jamal Tazi1,*

Institut de Génétique Moléculaire de Montpellier (IGM), UMR 5535 CNRS, Université Montpellier II, IFR 24, F34293 Montpellier Cedex 5,1 and Centre de Recherche de Biochimie Macromoléculaire, UPR 1086, IFR 24, F34293 Montpellier, Cedex 1,3 France; Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06536-08122; and University of California, San Diego, Department of Chemistry and Biochemistry, La Jolla, California 92093-03594

Received 21 June 2001/Returned for modification 17 July 2001/Accepted 23 August 2001

Mitogen activation of mRNA decay pathways likely involves specific endoribonucleases, such as G3BP, a phosphorylation-dependent endoribonuclease that associates with RasGAP in dividing but not quiescent cells. G3BP exclusively cleaves between cytosine and adenine (CA) after a specific interaction with RNA through the carboxyl-terminal RRM-type RNA binding motif. Accordingly, G3BP is tightly associated with a subset of poly(A)+ mRNAs containing its high-affinity binding sequence, such as the c-myc mRNA in mouse embryonic fibroblasts. Interestingly, c-myc mRNA decay is delayed in RasGAP-deficient fibroblasts, which contain a defective isoform of G3BP that is not phosphorylated at serine 149. A G3BP mutant in which this serine is changed to alanine remains exclusively cytoplasmic, whereas a glutamate for serine substitution that mimics the charge of a phosphorylated serine is translocated to the nucleus. Thus, a growth factor-induced change in mRNA decay may be modulated by the nuclear localization of a site-specific endoribonuclease such as G3BP.

* Corresponding author. Mailing address: Inst. de Gen. Mol. de Mont. (IGM), UMR 5535 CNRS, Université Montpellier II, CNRS, IFR 24, F34293 Montpellier Cedex 5, France. Phone: 33 (0) 4 67 61 36 85. Fax: 33 (0) 4 67 04 02 45. E-mail: tazi{at}igm.cnrs-mop.fr.

Molecular and Cellular Biology, November 2001, p. 7747-7760, Vol. 21, No. 22
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.22.7747-7760.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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