蛋白激酶C对人普列克底物蛋白丝氨酸-113和丝氨酸-117位点的磷酸化作用
Phosphorylation of human pleckstrin on Ser-113 and Ser-117 by protein kinase C.
作者信息
Craig K L, Harley C B
机构信息
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
出版信息
Biochem J. 1996 Mar 15;314 ( Pt 3)(Pt 3):937-42. doi: 10.1042/bj3140937.
Abstract
During platelet activation, receptor-coupled phospholipid hydrolysis stimulates protein kinase C (PKC) and results in the phosphorylation of several proteins, the most prominent being pleckstrin. Pleckstrin is composed of two repeated domains, now called pleckstrin homology (PH) domains, separated by a spacer region that contains several consensus PKC phosphorylation sites. To determine the role of PKC-dependent phosphorylation in pleckstrin function, we mapped the phosphorylation sites in vivo of wild-type and site-directed mutants of pleckstrin expressed in COS cells. Phosphorylation was found to occur almost exclusively on Ser-113 and Ser-117 within the sequence 108-KFARKSTRRSIRL-120. Phosphorylation of these sites was confirmed by phosphorylation of the corresponding wild-type and mutant synthetic peptides in vitro.
摘要
在血小板激活过程中，受体偶联的磷脂水解刺激蛋白激酶C（PKC），并导致几种蛋白质的磷酸化，其中最突出的是普列克底物蛋白。普列克底物蛋白由两个重复结构域组成，现在称为普列克底物蛋白同源（PH）结构域，由一个间隔区隔开，该间隔区包含几个一致的PKC磷酸化位点。为了确定PKC依赖性磷酸化在普列克底物蛋白功能中的作用，我们绘制了在COS细胞中表达的野生型和定点突变型普列克底物蛋白的体内磷酸化位点。发现磷酸化几乎只发生在序列108-KFARKSTRRSIRL-120中的Ser-113和Ser-117上。通过相应的野生型和突变型合成肽在体外的磷酸化证实了这些位点的磷酸化。
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