| Literature DB >> 21257758 |
Kristine E Kamm1, James T Stull.
Abstract
Myosin regulatory light chain (RLC) phosphorylation in skeletal and cardiac muscles modulates Ca(2+)-dependent troponin regulation of contraction. RLC is phosphorylated by a dedicated Ca(2+)-dependent myosin light chain kinase in fast skeletal muscle, where biochemical properties of RLC kinase and phosphatase converge to provide a biochemical memory for RLC phosphorylation and post-activation potentiation of force development. The recent identification of cardiac-specific myosin light chain kinase necessary for basal RLC phosphorylation and another potential RLC kinase (zipper-interacting protein kinase) provides opportunities for new approaches to study signaling pathways related to the physiological function of RLC phosphorylation and its importance in cardiac muscle disease.Entities:
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Year: 2011 PMID: 21257758 PMCID: PMC3060548 DOI: 10.1074/jbc.R110.198697
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157