TY - JOUR
T1 - RasGAP-associated endoribonuclease G3BP: Selective RNA degradation and phosphorylation-dependent localization
AU - Tourrière, H.
AU - Gallouzi, I. E.
AU - Chebli, K.
AU - Capony, J. P.
AU - Mouaikel, J.
AU - Van der Geer, P.
AU - Tazi, J.
N1 - Generated from Scopus record by KAUST IRTS on 2022-09-13
PY - 2001/11/1
Y1 - 2001/11/1
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 - https://journals.asm.org/doi/10.1128/MCB.21.22.7747-7760.2001
UR - http://www.scopus.com/inward/record.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
SN - 0270-7306
VL - 21
SP - 7747
EP - 7760
JO - Molecular and Cellular Biology
JF - Molecular and Cellular Biology
IS - 22
ER -