Journal
JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
Volume 30, Issue 1-2, Pages 67-72Publisher
SPRINGER
DOI: 10.1007/s10974-009-9176-y
Keywords
Cardiac troponin T; Raf-1; GW5074; Cardiomyocytes; Phosphorylation
Categories
Funding
- United States Public Health Service-National Heart, Lung and Blood Institute [HL-77860, HL-74161, AHA-SDG 0335199 N]
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Phosphorylation of cardiac troponin is a key mechanism involved in regulation of contractile function. In vitro kinase assays revealed that lysates prepared from resting cardiomyocytes contain cardiac troponin I (cTnI) and cTnT kinase activity. cTnI phosphorylation is inhibited by pharmacologic inhibitors of PKA, PKC, Rho kinase and PKC effectors such as RSK and PKD; these kinase inhibitors do not inhibit phosphorylation of cTnT. Rather, cTnT phosphorylation is decreased by the Raf inhibitor GW5074. In vitro kinase assays show that recombinant Raf phosphorylates cTnT, and that Raf-dependent cTnT phosphorylation is abrogated by a T206E substitution; Raf does not phosphorylate cTnI. These studies identify Raf-dependent cTnT-Thr(206) phosphorylation as a novel mechanism that would link growth factor-dependent signaling pathways to dynamic changes in cardiac contractile function.
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