Phosphorylation of Thr695 and Thr850 on the myosin phosphatase target subunit:: Inhibitory effects and occurrence in A7r5 cells
Phosphorylation of Thr695 and Thr850 on the myosin phosphatase target subunit:: Inhibitory effects and occurrence in A7r5 cells
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DOI：
10.1016/j.febslet.2005.10.055
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发表时间：
2005-12-05
期刊：
影响因子：
3.5
通讯作者：
Hartshorne, DJ
中科院分区：
文献类型：
--
作者：
Murányi, A;Derkach, D;Hartshorne, DJ
肌球蛋白磷酸酶靶亚基（MYPT 1）上Rho激酶的主要位点是Thr695和Thr850。Thr695的磷酸化抑制磷酸酶活性，但Thr850的磷酸化作用尚不清楚，本文对其进行了评价。Rho激酶对Thr695和Thr850的磷酸化抑制了I型磷酸酶催化亚基的活性。两个位点的磷酸化速率相似，磷酸化后的抑制功效对于每个位点是等同的。在A7r5细胞中检测到MYPT1上每个位点的磷酸化，但Thr850被Rho激酶优选，Thr695被未鉴定的激酶磷酸化。(c)2005年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
Major sites for Rho-kinase on the myosin phosphatase target subunit (MYPT1) are Thr695 and Thr850. Phosphorylation of Thr695 inhibits phosphatase activity but the role of phosphorylation at Thr850 is not clear and is evaluated here. Phosphorylation of both Thr695 and Thr850 by Rho-kinase inhibited activity of the type I phosphatase catalytic subunit. Rates of phosphorylation of the two sites were similar and efficacy of inhibition following phosphorylation was equivalent for each site. Phosphorylation of each site on MYPT1 was detected in A7r5 cells, but Thr850 was preferred by Rho-kinase and Thr695 was phosphorylated by an unidentified kinase(s). (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.