The small GTPases Rab5a, Rab5b and Rab5c are differentially phosphorylated in vitro
The small GTPases Rab5a, Rab5b and Rab5c are differentially phosphorylated in vitro
复制标题
DOI：
10.1016/s0014-5793(99)00686-9
复制
发表时间：
1999-06-18
期刊：
影响因子：
3.5
通讯作者：
Bucci, C
中科院分区：
文献类型：
--
作者：
Chiariello, M;Bruni, CB;Bucci, C
Rab GTPases在调节细胞膜运输中起着重要的作用。已经报道了三种不同的Rab5亚型，但在内吞作用中没有发现它们的功能差异。由于Rab5亚型显示出Ser/Thr磷酸化的保守共识位点，我们研究了该位点是否被磷酸化。在这里，我们报道了三种Rab5蛋白被不同的激酶识别的差异，Rab5a被细胞外调节激酶1有效磷酸化，而不被细胞外调节激酶2磷酸化，而cdc2激酶优先磷酸化Rab5b的Ser-123。这些发现有力地表明，磷酸化可能对Rab5异构体的差异调节功能很重要，(C) 1999年欧洲生化学会联合会。
Rab GTPases play a fundamental role in the regulation of membrane traffic. Three different Rab5 isoforms hare been reported but no differences in their function in endocytosis have been discovered. As the Rab5 isoforms show a conserved consensus site for Ser/Thr phosphorylation, we investigated whether this site was phosphorylated. Here, we report that the three Rab5 proteins are differentially recognized by different kinases, Rab5a is efficiently phosphorylated by extracellular-regulated kinase 1 but not by extracellular-regulated kinase 2, while cdc2 kinase preferentially phosphorylates Ser-123 of Rab5b. These findings strongly suggest that phosphorylation could be important to differentially regulate the function of the Rab5 isoforms, (C) 1999 Federation of European Biochemical Societies.