Mono- and consecutive bisphosphorylation of cTnI gradually reduces affinity to cTnC and cTnT by lowering association rate constants, while enhancing dissociation rate constants in ternary complexes.
Four phosphorylation degrees of cardiac troponin I (cTnI) have been characterized, namely, a dephospho, a bisphospho, and two monophospho states. Here we describe for the first time a role of the monophosphorylated forms. We have investigated the interaction between the cardiac troponin subunits dependent on the phosphorylation state of cTnI by surface plasmon resonance (SPR) spectroscopy. The monophosphorylated forms were generated by mutating each of the two serine residues, located in human cTnI at positions 22 and 23, to alanine. Association and dissociation rate constants of binary (cTnI-cTnT and cTnI-cTnC) and ternary (cTnI/cTnC complex-cTnT) complexes were determined. Mono- and consecutive bisphosphorylation of cTnI gradually reduces the affinity to cTnC and cTnT by lowering the association rate constants; the dissociation rate constants remain unchanged. Phosphorylation also affects formation of the ternary complexes; however, in this instance, association rate constants are constant, and dissociation rate constants are enhanced. A model of cardiac troponin is presented describing an induction of distinct conformational changes by mono- and bisphosphorylation of cTnI.
Reiffert et al. (Tue,) conducted a other in Cardiac troponin subunit interactions. Mono- and bisphosphorylation of cardiac troponin I (cTnI) vs. Dephospho state was evaluated on Association and dissociation rate constants of binary and ternary troponin complexes. Mono- and consecutive bisphosphorylation of cTnI gradually reduces affinity to cTnC and cTnT by lowering association rate constants, while enhancing dissociation rate constants in ternary complexes.
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