Role of the essential light chain in the activation of smooth muscle myosin by regulatory light chain phosphorylation
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چکیده
منابع مشابه
Quantitation of myosin light chain phosphorylation in intact smooth muscle.
An improved method for quantitating the extent of myosin light chain (P-LC) phosphorylation in small smooth muscle samples is described. Native myosin was isolated from other cellular proteins in a crude supernatant fraction prepared from a few milligrams of bovine tracheal smooth muscle by polyacrylamide gel electrophoresis (PAGE) in the presence of sodium pyrophosphate (PPi). When potassium i...
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Myosin light chain kinase phosphorylation in tracheal smooth muscle.
Purified myosin light chain kinase from smooth muscle is phosphorylated by cyclic AMP-dependent protein kinase, protein kinase C, and the multifunctional calmodulin-dependent protein kinase II. Because phosphorylation in a specific site (site A) by any one of these kinases desensitizes myosin light chain kinase to activation by Ca2+/calmodulin, kinase phosphorylation could play an important rol...
متن کاملStructural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase.
The substrate structure required for skeletal and smooth muscle myosin light chain kinases (MLC kinase) was studied by using various mutant regulatory light chains of smooth muscle myosin. The deletion of the NH2-terminal 10 residues did not greatly affect the kinetic parameters of smooth MLC kinase; however, deletion of an additional 3 residues, Lys11-Arg13, prevented phosphorylation. In contr...
متن کاملThe role of myosin light chain kinase phosphorylation in beta-adrenergic relaxation of tracheal smooth muscle.
Myosin light chain kinase from smooth muscle has been shown to be phosphorylated by cyclic AMP-dependent protein kinase, which leads to a decrease in the affinity of the kinase for Ca2+ . calmodulin and, hence, a decrease in enzymatic activity. This event has been proposed as a mechanism for the relaxation of smooth muscle in response to increased intracellular concentrations of cyclic AMP. The...
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ژورنال
عنوان ژورنال: Journal of Structural Biology
سال: 2014
ISSN: 1047-8477
DOI: 10.1016/j.jsb.2013.12.008