Phosphorylation and actin activation of brain myosin.
نویسندگان
چکیده
منابع مشابه
Effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation.
A 35--70% ammonium sulfate fraction of smooth muscle actomyosin was prepared from guinea pig vas deferens. This fraction also contains a smooth muscle myosin kinase and a phosphatase that phosphorylates and dephosphorylates, respectively, the 20,000-dalton light chain of smooth muscle myosin. Phosphorylated and dephosphorylated smooth muscle myosin. Phosphorylated and dephosphorylated smooth mu...
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A variety of contractile stimuli increases actin polymerization, which is essential for smooth muscle contraction. However, the mechanism(s) of actin polymerization associated with smooth muscle contraction is not fully understood. We tested the hypothesis that phosphorylated myosin triggers actin polymerization. The present study was conducted in isolated intact or beta-escin-permeabilized rat...
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Brain actin extracted from an acetone powder of chick brains was purified by a cycle of polymerization-depolymerization followed by molecular sieve chromatography. The brain actin had a subunit molecular weight of 42,000 daltons as determined by co-electrophoresis with muscle actin. It underwent salt-dependent g to f transformation to form double helical actin filaments which could be "decorate...
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It has been demonstrated previously that during mitosis the sites of myosin phosphorylation are switched between the inhibitory sites, Ser 1/2, and the activation sites, Ser 19/Thr 18 (Yamakita, Y., S. Yamashiro, and F. Matsumura. 1994. J. Cell Biol. 124:129- 137; Satterwhite, L.L., M.J. Lohka, K.L. Wilson, T.Y. Scherson, L.J. Cisek, J.L. Corden, and T.D. Pollard. 1992. J. Cell Biol. 118:595-60...
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The 20,000-dalton light chain of myosin from chicken gizzard has been shown to be phosphorylated in a Ca’+ and calmodulin-independent manner by the activated form of a protease-activated kinase from rabbit reticulocytes. Protease-activated kinase I incorporates phosphate stoichiometrically into the phosphorylatable light chain (P-light chain) in isolated myosin light chains and in actomyosin...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 1983
ISSN: 0261-4189
DOI: 10.1002/j.1460-2075.1983.tb01432.x