Dephosphorylation of myosin regulatory light chain negatively modulates actomyosin dissociation and positively influences actomyosin ATPase activity, which is adverse to meat tenderness.
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Suggests a mechanistic link between myosin dephosphorylation and muscle rigidity; leaves open whether targeting this.
Summary The objective of this study was to investigate the relationship between the dephosphorylation of myosin regulatory light chain and actin–myosin interaction after muscle homogenate was treated with alkaline phosphatase and phosphatase inhibitor. The myosin regulatory light chain was significantly dephosphorylated by alkaline phosphatase after incubation. Among different groups, dephosphorylated myosin regulatory light chain to a much greater extent leads to a lower actomyosin dissociation degree, thereby raising the actomyosin ATPase activity, whereas it exhibits a higher actomyosin dissociation degree and a lower actomyosin ATPase activity when the myosin regulatory light chain was in a low dephosphorylated state. The data suggest that the dephosphorylation of myosin regulatory light chain modulates actomyosin dissociation (the number of myosin interact with actin) negatively and has a positive influence on actomyosin ATPase activity (the interacting force between myosin and actin).
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Gao et al. (2017) studied this question.
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