Abstract
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.
Original language | English (US) |
---|---|
Pages (from-to) | 9941-9947 |
Number of pages | 7 |
Journal | Journal of Biological Chemistry |
Volume | 286 |
Issue number | 12 |
DOIs | |
State | Published - Mar 25 2011 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology