RasGAP-associated endoribonuclease G3BP

Selective RNA degradation and phosphorylation-dependent localization

H. Tourrière, Imed Gallouzi, K. Chebli, J. P. Capony, J. Mouaikel, P. Van der Geer, J. Tazi

Research output: Contribution to journalArticle

117 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)7747-7760
Number of pages14
JournalMolecular and Cellular Biology
Volume21
Issue number22
DOIs
Publication statusPublished - 2001
Externally publishedYes

Fingerprint

Endoribonucleases
RNA Stability
Serine
Phosphorylation
Fibroblasts
Messenger RNA
Cytosine
Adenine
Mitogens
Alanine
Glutamic Acid
Intercellular Signaling Peptides and Proteins
Protein Isoforms
RNA

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

RasGAP-associated endoribonuclease G3BP : Selective RNA degradation and phosphorylation-dependent localization. / Tourrière, H.; Gallouzi, Imed; Chebli, K.; Capony, J. P.; Mouaikel, J.; Van der Geer, P.; Tazi, J.

In: Molecular and Cellular Biology, Vol. 21, No. 22, 2001, p. 7747-7760.

Research output: Contribution to journalArticle

Tourrière, H. ; Gallouzi, Imed ; Chebli, K. ; Capony, J. P. ; Mouaikel, J. ; Van der Geer, P. ; Tazi, J. / RasGAP-associated endoribonuclease G3BP : Selective RNA degradation and phosphorylation-dependent localization. In: Molecular and Cellular Biology. 2001 ; Vol. 21, No. 22. pp. 7747-7760.
@article{6d922bdf83944102a4b4bd544cd08945,
title = "RasGAP-associated endoribonuclease G3BP: Selective RNA degradation and phosphorylation-dependent localization",
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.",
author = "H. Tourri{\`e}re and Imed Gallouzi and K. Chebli and Capony, {J. P.} and J. Mouaikel and {Van der Geer}, P. and J. Tazi",
year = "2001",
doi = "10.1128/MCB.21.22.7747-7760.2001",
language = "English",
volume = "21",
pages = "7747--7760",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "American Society for Microbiology",
number = "22",

}

TY - JOUR

T1 - RasGAP-associated endoribonuclease G3BP

T2 - Selective RNA degradation and phosphorylation-dependent localization

AU - Tourrière, H.

AU - Gallouzi, Imed

AU - Chebli, K.

AU - Capony, J. P.

AU - Mouaikel, J.

AU - Van der Geer, P.

AU - Tazi, J.

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0034775591&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034775591&partnerID=8YFLogxK

U2 - 10.1128/MCB.21.22.7747-7760.2001

DO - 10.1128/MCB.21.22.7747-7760.2001

M3 - Article

VL - 21

SP - 7747

EP - 7760

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 22

ER -