Functional dissection of myosin binding protein C phosphorylation.

ABSTRACT: Cardiac myosin binding protein C (cMyBP-C) phosphorylation is differentially regulated in the normal heart and during disease development. Our objective was to examine in detail three phosphorylatable sites (Ser-273, Ser-282, and Ser-302) present in the protein's cardiac-specific sequences, as these residues are differentially and reversibly phosphorylated during normal and abnormal cardiac function. Three transgenic lines were generated: DAA, which expressed cMyBP-C containing Asp-273, Ala-282, and Ala-302, in which a charged amino acid was placed at residue 273 and the remaining two sites rendered nonphosphorylatable by substituting alanines for the two serines; AAD containing Ala-273, Ala-282, and Asp-302, in which aspartate was placed at residue 302 and the remaining two sites rendered

SUBMITTER: Gupta MK 

PROVIDER: S-EPMC3847820 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature