Myosin Light Chain Phosphatase

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Myosin light-chain phosphatase.

1. A method for the isolation of a new enzyme, myosin light-chain phosphatase, from rabbit white skeletal muscle by using a Sepharose-phosphorylated myosin light-chain affinity column is described. 2. The enzyme migrated as a single component on electrophoresis in sodium dodecyl sulphate/polyacrylamide gel at pH7.0, with apparent mol.wt. 70000. 3. The enzyme was highly specific for the phosphor...

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Myosin light chain phosphatase: it gets around.

The importance of Ca 2 /calmodulin-dependent myosin light chain kinase (MLCK) for smooth muscle contraction is well documented.1 Until recently, myosin light chain (MLC) phosphatase was thought to be unregulated and constitutively active. However, studies have demonstrated that smooth muscle contraction is dependent on regulation of MLC phosphatase activity.2,3 The inhibition of phosphatase act...

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Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function

We have partially purified myosin light chain kinase (MLCK) and myosin light chain phosphatase (MLCP) from Dictyostelium discoideum. MLCK was purified 4,700-fold with a yield of approximately 1 mg from 350 g of cells. The enzyme is very acidic as suggested by its tight binding to DEAE. Dictyostelium MLCK has an apparent native molecular mass on HPLC G3000SW of approximately 30,000 D. Mg2+ is re...

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Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis.

Contractile actomyosin networks generate forces that drive tissue morphogenesis. Actomyosin contractility is controlled primarily by reversible phosphorylation of the myosin-II regulatory light chain through the action of myosin kinases and phosphatases. While the role of myosin light-chain kinase in regulating contractility during morphogenesis has been largely characterized, there is surprisi...

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Myosin light chain phosphatase: a Cinderella of cellular signaling.

Although several myofilament proteins are modified by protein phosphorylation, the 18-kDa myosin light chain 2 (MLC2) has special significance. In striated muscle, after some experimental struggles, MLC2 phosphorylation was shown to modulate myofilament activation by Ca.1 However, in the case of smooth muscle, phosphorylation of the MLC2 by a Ca calmodulin–dependent kinase triggers contraction....

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ژورنال

عنوان ژورنال: Circulation Research

سال: 2002

ISSN: 0009-7330,1524-4571

DOI: 10.1161/01.res.0000014224.43774.03