Biochemistry of smooth muscle myosin light chain kinase.

Biochemistry of smooth muscle myosin light chain kinase.
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DOI:
10.1016/j.abb.2011.04.018
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发表时间:
2011-06-15
影响因子:
3.9
通讯作者:
Cremo, Christine R.
Cremo, Christine R.
中科院分区:
生物学3区
文献类型:
--
作者:
Hong, Feng;Haldeman, Brian D.;Jackson, Del;Carter, Mike;Baker, Jonathan E.;Cremo, Christine R.

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肌球蛋白轻链激酶 (MLCK) 的平滑肌亚型是一种 Ca2+-钙调蛋白激活激酶,存在于许多组织中。它对于通过肌球蛋白磷酸化调节平滑肌收缩尤其重要。这篇综述总结了近期 MLCK 生化工作中与其在平滑肌中的功能相关的选定方面。一般来说,审查的重点是新的发现、未解决的问题以及需要进一步研究的具有高度生理意义的潜力的领域。该综述包括对结构、底物和酶活性的简要总结,然后讨论了可能限制 MLCK 在肌肉中有效活性的因素。总结了 MLCK 的多个结构域中的每一个与收缩装置蛋白质的相互作用,以及可能控制其在细胞中行为的 MLCK 的多结构域相互作用。最后,介绍了研究肌球蛋白磷酸化机制的新体外方法。
The smooth muscle isoform of myosin light chain kinase (MLCK) is a Ca2+-calmodulin-activated kinase that is found in many tissues. It is particularly important for regulating smooth muscle contraction by phosphorylation of myosin. This review summarizes selected aspects of recent biochemical work on MLCK that pertains to its function in smooth muscle. In general, the focus of the review is on new findings, unresolved issues, and areas with the potential for high physiological significance that need further study. The review includes a concise summary of the structure, substrates, and enzyme activity, followed by a discussion of the factors that may limit the effective activity of MLCK in the muscle. The interactions of each of the many domains of MLCK with the proteins of the contractile apparatus, and the multi-domain interactions of MLCK that may control its behaviors in the cell are summarized. Finally, new in vitro approaches to studying the mechanism of phosphorylation of myosin are introduced.
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