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• W1989527553 abstract "The significance of site-specific phosphorylation by protein kinase C (PKC) isozymes α and δ and protein kinase A (PKA) of troponin I (TnI) and its phosphorylation site mutants in the regulation of Ca2+-stimulated MgATPase activity of reconstituted actomyosin S-1 was investigated. The genetically defined TnI mutants used were T144A, S43A/S45A, S43A/S45A/T144A (in which the PKC phosphorylation sites Thr-144 and Ser-43/Ser-45 were respectively substituted by Ala) and N32 (in which the first 32 amino acids in the NH2-terminal sequence containing Ser-23/Ser-24 were deleted). Although the PKC isozymes displayed different substrate phosphorylation kinetics, PKC-α phosphorylated equally well TnI wild type and all mutants, whereas N32 was a much poorer substrate for PKC-δ. Furthermore, the two PKC isozymes exhibited discrete specificities in phosphorylating distinct sites in TnI and its mutants, either as individual subunits or as components of the reconstituted troponin complex. Unlike PKC-α, PKC-δ favorably phosphorylated the PKA-preferred site Ser-23/Ser-24 and hence, like PKA, reduced the Ca2+ sensitivity of the reconstituted actomyosin S-1 MgATPase. In contrast, PKC-α preferred to phosphorylate Ser-43/Ser-45 (common sites for all isozymes) and thus reduced the maximal Ca2+-stimulated activity of the MgATPase. In this respect, PKC-δ, by cross-phosphorylating the PKA sites, functioned as a hybrid of PKC-α and PKA. The site specificities and hence functional differences between PKC-α and -δ were most evident at low phosphorylation (1 mol of phosphate/mol) of TnI wild type and were magnified when S43A/S45A and N32 were used as substrates. The present study has demonstrated, for the first time, that distinct functional consequences could arise from the site-selective preferences of PKC-α and -δ for phosphorylating a single substrate in the myocardium, i.e., TnI." @default.
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• W1989527553 date "1996-01-01" @default.
• W1989527553 modified "2023-09-26" @default.
• W1989527553 title "Differential Regulation of Cardiac Actomyosin S-1 MgATPase by Protein Kinase C Isozyme-Specific Phosphorylation of Specific Sites in Cardiac Troponin I and Its Phosphorylation Site Mutants" @default.
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• W1989527553 doi "https://doi.org/10.1021/bi9616357" @default.
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