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• W2056527627 abstract "Phosphorylation and Ca2+–Mg2+ exchange on the regulatory light chains (RLCs) of skeletal myosin modulate muscle contraction. However, the relation between the mechanisms for the effects of phosphorylation and metal ion exchange are not clear. We propose that modulation of skeletal muscle contraction by phosphorylation of the myosin regulatory light chains (RLCs) is mediated by altered electrostatic interactions between myosin heads/necks and the negatively charged thick filament backbone. Our study, using the in vitro motility assay, showed actin motility on hydrophilic negatively charged surfaces only over the HMM with phosphorylated RLCs both in the presence and absence of Ca2+. In contrast, good actin motility was observed on silanized surfaces (low charge density), independent of RLC phosphorylation status but with markedly lower velocity in the presence of Ca2+. The data suggest that Ca2+-binding to, and phosphorylation of, the RLCs affect the actomyosin interaction by independent molecular mechanisms. The phosphorylation effects depend on hydrophobicity and charge density of the underlying surface. Such findings might be exploited for control of actomyosin based transportation of cargoes in lab-on-a chip applications, e.g. local and temporary stopping of actin sliding on hydrophilic areas along a nanosized track." @default.
• W2056527627 created "2016-06-24" @default.
• W2056527627 creator A5003694914 @default.
• W2056527627 creator A5017515663 @default.
• W2056527627 date "2010-12-01" @default.
• W2056527627 modified "2023-09-27" @default.
• W2056527627 title "Regulatory light chains modulate in vitro actin motility driven by skeletal heavy meromyosin" @default.
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• W2056527627 doi "https://doi.org/10.1016/j.bbrc.2010.10.039" @default.
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