Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin
Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin
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DOI：
10.1016/s0014-5793(02)03175-7
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发表时间：
2002-09-11
期刊：
影响因子：
3.5
通讯作者：
Cohen, P
中科院分区：
文献类型：
--
作者：
Velasco, G;Armstrong, C;Cohen, P
已知Rho激酶通过磷酸化肌球蛋白相关形式的蛋白磷酸酶1（PP1M）的110 kDa肌球蛋白靶向亚基（MYPT 1）来控制平滑肌收缩性。先前已报道MYPT1在Thr695处的磷酸化抑制PP1的催化活性。在这里，我们表明，Thr850的磷酸化Rho激酶解离PP1M肌球蛋白，提供了第二种机制，肌球蛋白磷酸酶活性被抑制。(C)2002年欧洲生物化学学会联合会。
Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited. (C) 2002 Federation of European Biochemical Societies.