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. 1993 Mar 1;290(Pt 2):437–442. doi: 10.1042/bj2900437

Phosphorylation by casein kinase II affects the interaction of caldesmon with smooth muscle myosin and tropomyosin.

N V Bogatcheva 1, A V Vorotnikov 1, K G Birukov 1, V P Shirinsky 1, N B Gusev 1
PMCID: PMC1132292  PMID: 8452532

Abstract

Smooth muscle caldesmon was phosphorylated by casein kinase II, and the effects of phosphorylation on the interaction of caldesmon and its chymotryptic peptides with myosin and tropomyosin were investigated. The N-terminal chymotryptic peptide of caldesmon of molecular mass 27 kDa interacted with myosin. Phosphorylation of Ser-73 catalysed by casein kinase II resulted in a 2-fold decrease in the affinity of the native caldesmon (or its 27 kDa N-terminal peptide) for smooth muscle myosin. At low ionic strength, caldesmon and its N-terminal peptides of molecular masses 25 and 27 kDa were retarded on a column of immobilized tropomyosin. Phosphorylation of Ser-73 led to a 2-4-fold decrease in the affinity of caldesmon (or its N-terminal peptides) for tropomyosin. Thus phosphorylation of Ser-73 catalysed by casein kinase II affects the interaction of caldesmon with both smooth muscle myosin and tropomyosin.

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Selected References

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