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Cardiac Myosin Light Chain - Europe PMC

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Last Updated: 16 August 2022

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Myosin light chain phosphatase catalytic subunit dephosphorylates cardiac myosin via mechanisms dependent and independent of the MYPT regulatory subunits.

In normal hearts, the myosin regulatory light chain is phosphorylated at u223c0. 4 mol phosphate/mol RLC, and phosphorylation is maintained by balanced usage of dedicated cardiac muscle-specific myosin light chain kinase and phosphatase. In vivo, smooth muscle contractions can be performed by MYPT1 and PP1c;u03b2 co-stabilize each other, and are both essential for normal smooth muscle contractions. MYPT1 and MYPT2 have both been expressed in the cardiac muscle, but the contributions to physiological control of cardiac myosin dephosphorylation are uncertain. Both myosin-targeted and soluble MYPT1c. u03b2 proteins in vivo are not dependent on cellular expression, while 2 cardiac muscle pathogenesis in PP1c and non-muscle cells, 3 the stability of cardiac MYPT1c and MYPT2 proteins in vivo is not dependent on the PP1c:u03b2 protein is not dependent on mouse and non-muscle cells, 2 cardiac muscle pathogenesis in u03b2 phosphatedib1cu03b2 protein phosphate in phosphate3b2 protein dephosphorylated phosphatet1cu03b1cu03b2 knockout mice b2u03b2u03b2 protein 1 cu03b1cu03b2 u03b2u03b2 protein cu03b2u03b2u03b2u03b2u03b1cu03b2u03b2u03b2u.

Source link: https://europepmc.org/article/MED/35872014


Hypertrophic cardiomyopathy mutations in the pliant and light chain-binding regions of the lever arm of human β-cardiac myosin have divergent effects on myosin function.

Both motor performance and myosin subfragment 2 tail-based autoinhibition were investigated by our researchers. The actin detachment rate increased power output, L781P reduced power production, and S782N had no effect on power output, although all three mutations altered the external force sensitivity of the actin detachment rate. With a myosin containing the motor domain and the proximal S2 tail, the pliant region mutations also tempered autoinhibition in the presence of filamentous actin, but had no effect in the absence of actin. Thus, mutations in the lever arm of u03b-cardiac myosin may have divergent allosteric effects on myosin function, depending on whether they are in the pliant or light chain-binding regions.

Source link: https://europepmc.org/article/MED/35767336

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions