Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C.
Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C.
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DOI：
10.1021/bi00410a024
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发表时间：
1988-05
期刊：
影响因子：
2.9
通讯作者：
L. Varticovski;S. Chahwala;M. Whitman;L. Cantley;Daniel Schindler-;E. Chow;L. K. Sinclair;R. Pepinsky
中科院分区：
文献类型：
--
作者：
L. Varticovski;S. Chahwala;M. Whitman;L. Cantley;Daniel Schindler-;E. Chow;L. K. Sinclair;R. Pepinsky
脂皮质素I是一种39千道尔顿的膜相关蛋白，在A431细胞中，其响应于表皮生长因子（EGF）而在酪氨酸上磷酸化。我们已经使用重组人脂皮质素I作为底物的几种蛋白激酶，并确定磷酸化残基的肽映射和序列分析的组合。脂皮质素I在Tyr-21的氨基末端附近被重组pp 60 c-src磷酸化。相同的酪氨酸残基被多瘤中间T/pp 60 c-src复合物磷酸化，被重组pp 50 v-abl磷酸化，并被EGF受体/激酶与A431细胞膜磷酸化。蛋白激酶C磷酸化的主要位点也靠近丝氨酸-27的氨基末端。腺苷环3 '，5'-磷酸依赖性蛋白激酶磷酸化的主要位点在分子的羧基末端的一半，在Thr-216。将这些位点与先前位于结构相关蛋白脂皮质素II中的磷酸化位点进行比较。
Lipocortin I is a 39-kilodalton membrane-associated protein that in A431 cells is phosphorylated on tyrosine in response to epidermal growth factor (EGF). We have used recombinant human lipocortin I as a substrate for several protein kinases and identified phosphorylated residues by a combination of peptide mapping and sequence analysis. Lipocortin I was phosphorylated near the amino terminus at Tyr-21 by recombinant pp60c-src. The same tyrosine residue was phosphorylated by polyoma middle T/pp60c-src complex, by recombinant pp50v-abl, and with A431 cell membranes by the EGF receptor/kinase. The primary site of phosphorylation by protein kinase C was also near the amino terminus at Ser-27. The major site of phosphorylation by adenosine cyclic 3',5'-phosphate dependent protein kinase was on the carboxy-terminal half of the molecule at Thr-216. These sites are compared to the phosphorylation sites previously located in the structurally related protein lipocortin II.