Activation of Smooth Muscle Myosin Light Chain Kinase by Calmodulin
نویسندگان
چکیده
منابع مشابه
Regulation of smooth muscle myosin light chain kinase. Allosteric effects and co-operative activation by calmodulin.
The activation of smooth muscle myosin light chain kinase (MLCKase) by calcium and calmodulin (CM) was investigated over a wide range of concentrations of the enzyme using myosin (MY) or its isolated phosphorylatable light chain (L20) as substrates. The enzyme showed allosteric behavior. The specific phosphorylation activity was dependent on the concentration of MLCKase as well as on the concen...
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Myosin light-chain kinase (MLCK) of smooth muscle is multifunctional, being composed of N-terminal actin-binding domain, central kinase domain, and C-terminal myosin-binding domain. The kinase domain is the best characterized; this domain activates the interaction of smooth-muscle myosin with actin by phosphorylating the myosin light chain. We have recently shown that the Met-1-Pro-41 sequence ...
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Calmodulin (CaM)-dependent myosin light chain kinase (MLCK) plays a key role in activation of smooth muscle contraction. A soybean isoform of CaM, SCaM-4 (77% identical to human CaM) fails to activate MLCK, whereas SCaM-1 (90.5% identical to human CaM) is as effective as CaM. We exploited this difference to gain insights into the structural requirements in CaM for activation of MLCK. A chimera ...
متن کاملThe calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence.
Smooth muscle myosin light chain kinase contains a 64 residue sequence that binds calmodulin in a Ca2+-dependent manner (Guerriero, V., Jr., Russo, M. A., and Means, A. R. (1987) Biochemistry, in press). Within this region is a sequence with homology to the corresponding sequence reported for the calmodulin binding region of skeletal muscle myosin light chain kinase (Blumenthal, D. K., Takio, K...
متن کاملPurification and characterization of smooth muscle myosin light chain kinase.
Smooth muscle myosin light chain kinase was purified from turkey gizzards. The enzyme was extracted from washed myofibrils and the final step of purification was affinity chromatography using calmodulin coupled to Sepharose 4B. The purified enzyme was characterized with respect to its physical, chemical, and kinetic properties. It has a molecular weight of 130,000 by sodium dodecyl sulfate poly...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m111404200