Phosphorylation by casein kinase II affects the interaction of caldesmon with smooth muscle myosin and tropomyosin
| Autor: | Nikolai B. Gusev, Natalia V. Bogatcheva, Konstantin G. Birukov, V.P. Shirinsky, Alexander V. Vorotnikov |
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| Rok vydání: | 1993 |
| Předmět: |
animal structures
Peptide Tropomyosin macromolecular substances Myosins Protein Serine-Threonine Kinases Biochemistry Myosin Animals Phosphorylation Casein Kinase II Molecular Biology chemistry.chemical_classification biology Molecular mass Chemistry Binding protein Muscle Smooth Cell Biology musculoskeletal system Caldesmon Ducks Liver biology.protein Calmodulin-Binding Proteins Rabbits Casein kinase 2 Research Article |
| Zdroj: | Biochemical Journal. 290:437-442 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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