Regulation of myosin phosphatase by Rho and Rho-Associated kinase (Rho-kinase)
Regulation of myosin phosphatase by Rho and Rho-Associated kinase (Rho-kinase)
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DOI：
10.1126/science.273.5272.245
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发表时间：
1996-07-12
期刊：
影响因子：
56.9
通讯作者：
Kaibuchi, K
中科院分区：
文献类型：
--
作者：
Kimura, K;Ito, M;Kaibuchi, K
小分子鸟苷三磷酸酶Rho与肌球蛋白轻链（MLC）的磷酸化有关，这会导致平滑肌收缩以及非肌细胞中肌动蛋白和肌球蛋白的相互作用。与鸟苷三磷酸（GTP）结合的RhoA活性形式（GTP·RhoA）特异性地与肌球蛋白磷酸酶的肌球蛋白结合亚基（MBS）相互作用，该亚基调节MLC的磷酸化程度。由GTP·RhoA激活的Rho相关激酶（Rho - 激酶）使MBS磷酸化，从而使肌球蛋白磷酸酶失活。在NIH 3T3细胞中RhoA或激活的RhoA的过表达增加了MBS和MLC的磷酸化。因此，Rho似乎通过Rho - 激酶的作用抑制肌球蛋白磷酸酶。
The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP . RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP . RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.