生物物理
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
総説
ミオシンホスファターゼ阻害タンパク質 CPI-17の構造と機能
大木 進野江藤 真澄松澤 史子甲斐荘 正恒
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2005 年 45 巻 2 号 p. 72-77

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Cell motility, including smooth muscle contraction and cell migration, is regulated by reversible phosphorylation of myosin. Recent studies have shown that myosin phosphatase (MP), along with kinases, contributes dynamically to the regulation of myosin-II phosphorylation. An MP specific inhibitor named CPI-17, which is expressed in smooth muscle and neuronal cells, mediates receptor signaling leading to myosin-II phosphorylation. In this review, we discuss structure/function relationships of CPI-17 stemming from our recent NMR studies and computer modeling results. The combination of biophysical approaches with biochemical techniques has revealed the inhibitory mechanism of CPI-17.

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© 2005 by THE BIOPHYSICAL SOCIETY OF JAPAN
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