GAP-SH3结合蛋白的一种新型磷酸化依赖性核糖核酸酶活性：信号转导与RNA稳定性之间的潜在联系。
A novel phosphorylation-dependent RNase activity of GAP-SH3 binding protein: a potential link between signal transduction and RNA stability.
作者信息
Gallouzi I E, Parker F, Chebli K, Maurier F, Labourier E, Barlat I, Capony J P, Tocque B, Tazi J
机构信息
Institut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, Université Montpellier II, F34293 Montpellier Cedex 5, France.
出版信息
Mol Cell Biol. 1998 Jul;18(7):3956-65. doi: 10.1128/MCB.18.7.3956.
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.
摘要
一种潜在的p120 GTP酶激活蛋白（RasGAP）效应器，G3BP（RasGAP Src同源3 [SH3]结合蛋白），先前是基于其与RasGAP的SH3结构域结合的能力而被鉴定出来的。在这里我们表明，在血清刺激的而非静止的中国仓鼠肺成纤维细胞的质膜上，G3BP与RasGAP共定位并发生物理相互作用。在静止细胞中，G3BP在丝氨酸残基上发生高度磷酸化，这种修饰对其活性至关重要。实际上，G3BP具有一种磷酸化依赖性核糖核酸酶活性，它能特异性切割人c-myc mRNA的3'非翻译区。G3BP的核糖核酸内切酶活性可启动mRNA降解，因此代表了RasGAP介导的信号通路与RNA周转之间的一种联系。
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The Ras-GTPase-activating protein SH3 domain is required for Cdc2 activation and mos induction by oncogenic Ras in Xenopus oocytes independently of mitogen-activated protein kinase activation.Ras鸟苷三磷酸酶激活蛋白的SH3结构域是非洲爪蟾卵母细胞中致癌性Ras激活Cdc2及诱导mos所必需的，且不依赖于丝裂原活化蛋白激酶的激活。
Mol Cell Biol. 1996 Jun;16(6):3179-86. doi: 10.1128/MCB.16.6.3179.
10
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