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PMID: 11604510 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization.

Molecular and cellular biology ·Vol. 21 ·No. 22 ·2001-11-00 ·Pages 7747-60

Tourrière H, Gallouzi IE, Chebli K, Capony JP, Mouaikel J, van der Geer P, Tazi J

Abstract

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.

MeSH Terms
3' Untranslated Regions/metabolism Amino Acid Substitution Animals Base Sequence Binding Sites Carrier Proteins/genetics,metabolism Cell Nucleus/metabolism Cells, Cultured Cytoplasm/metabolism DNA Helicases Endoribonucleases/genetics,metabolism Fibroblasts/cytology Glutamic Acid/genetics,metabolism Isoenzymes/genetics,metabolism Mice Mice, Knockout Molecular Sequence Data Mutagenesis, Site-Directed Phosphorylation Poly-ADP-Ribose Binding Proteins Proto-Oncogene Proteins c-myc/genetics RNA Helicases RNA Recognition Motif Proteins RNA, Messenger/metabolism Serine/genetics,metabolism Substrate Specificity p120 GTPase Activating Protein/genetics,metabolism
Chemicals
3' Untranslated Regions Carrier Proteins Isoenzymes Poly-ADP-Ribose Binding Proteins Proto-Oncogene Proteins c-myc RNA Recognition Motif Proteins RNA, Messenger p120 GTPase Activating Protein Glutamic Acid Serine Endoribonucleases DNA Helicases G3bp1 protein, mouse RNA Helicases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Tourrière H
Institut de Génétique Moléculaire de Montpellier (IGM), UMR 5535 CNRS, Université Montpellier II, IFR 24, F34293 Montpellier Cedex 5, France.
Gallouzi I E
Chebli K
Capony J P
Mouaikel J
van der Geer P
Tazi J
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.21.22.7747-7760.2001
Published
2001-11-00
Pages
7747-60
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC99945
Subset
IM
External Links
PubMed source DOI: 10.1128/MCB.21.22.7747-7760.2001 PMC Full Text View journal details
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