Actin-induced Closure of the Actin-binding Cleft of Smooth Muscle Myosin
نویسندگان
چکیده
منابع مشابه
Actin-induced closure of the actin-binding cleft of smooth muscle myosin.
The putative actin-binding interface of myosin is separated by a large cleft that extends into the base of the nucleotide binding pocket, suggesting that it may be important for mediating the nucleotide-dependent changes in the affinity for myosin on actin. We have genetically engineered a truncated version of smooth muscle myosin containing the motor domain and the essential light chain-bindin...
متن کاملThe binding of smooth muscle myosin light chain kinase and phosphatases to actin and myosin.
Contractile activity in smooth muscle cells is regulated by phosphorylation-dephosphorylation of the 20,000-Da light chain of myosin. In an attempt to better understand the localization in muscle of the enzymes which catalyze the phosphorylation-dephosphorylation process, we measured the binding constants of turkey gizzard smooth muscle myosin light chain (MLC) kinase and smooth muscle phosphat...
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Phosphorylation of the regulatory light chain of smooth muscle myosin efficiently regulates the actin-activated ATPase activity of myosin filaments in solution and actin movement in an in vitro motility assay, independently of thin-filament regulatory proteins. Filaments containing both phosphorylated and dephosphorylated heads move actin at intermediate rates, depending on the relative proport...
متن کاملActin-binding cleft closure in myosin II probed by site-directed spin labeling and pulsed EPR.
We present a structurally dynamic model for nucleotide- and actin-induced closure of the actin-binding cleft of myosin, based on site-directed spin labeling and electron paramagnetic resonance (EPR) in Dictyostelium myosin II. The actin-binding cleft is a solvent-filled cavity that extends to the nucleotide-binding pocket and has been predicted to close upon strong actin binding. Single-cystein...
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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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m111253200