Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Iα
Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Iα
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DOI：
10.1126/science.286.5444.1583
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发表时间：
1999-11-19
期刊：
影响因子：
56.9
通讯作者：
Mendelsohn, ME
中科院分区：
文献类型：
--
作者：
Surks, HK;Mochizuki, N;Mendelsohn, ME
肌凝蛋白轻链激酶和肌凝蛋白磷酸酶通过肌凝蛋白轻链的磷酸化和去磷酸化调节平滑肌的收缩和舒张。环鸟苷单磷酸（cGMP）依赖性蛋白激酶I α (cGKI α)介导血管平滑肌对一氧化氮和cGMP的生理性松弛。研究表明，cGKI α通过与肌球蛋白磷酸酶的肌球蛋白结合亚基（MBS）的亮氨酸拉链相互作用靶向平滑肌细胞收缩装置。解偶联的cGKI α - mbs相互作用阻止了cgmp依赖性肌球蛋白轻链的去磷酸化，表明这种相互作用对血管平滑肌细胞张力的调节至关重要。
Contraction and relaxation of smooth muscle are regulated by myosin light-chain kinase and myosin phosphatase through phosphorylation and dephosphorylation of myosin light chains. Cyclic guanosine monophosphate (cGMP)-dependent protein kinase I alpha (cGKI alpha) mediates physiologic relaxation of vascular smooth muscle in response to nitric oxide and cGMP. It is shown here that cGKI alpha is targeted to the smooth muscle cell contractile apparatus py a Leucine zipper interaction with the myosin-binding subunit (MBS) of myosin phosphatase. Uncoupling of the cGKI alpha-MBS interaction prevents cGMP-dependent dephosphorylation of myosin light chain, demonstrating that this interaction is essential to the regulation of vascular smooth muscle cell tone.