Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 12, Pages 9941-9947Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R110.198697
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Funding
- National Institutes of Health [HL080536, HL026043]
- Moss Heart Fund
- Fouad A. and Val Imm Bashour Distinguished Chair in Physiology
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Myosin regulatory light chain (RLC) phosphorylation in skeletal and cardiac muscles modulates Ca2+-dependent troponin regulation of contraction. RLC is phosphorylated by a dedicated Ca2+-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.
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