Phosphorylation of dystrophin:effects on actin binding
| Autor: | G. Salviati, S. Ceoldo, L. Senter, M. Meznaric Petrusa |
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| Rok vydání: | 1995 |
| Předmět: |
inorganic chemicals
Biophysics macromolecular substances Protein Serine-Threonine Kinases environment and public health Biochemistry MAP2K7 Dystrophin Sarcolemma Utrophin Animals Protein phosphorylation Actin-binding protein Phosphorylation Casein Kinase II Muscle Skeletal Molecular Biology Protein kinase C Protein Kinase C biology Chemistry Cyclin-dependent kinase 5 Cell Membrane Cell Biology Actin cytoskeleton Cyclic AMP-Dependent Protein Kinases Actins enzymes and coenzymes (carbohydrates) Kinetics biology.protein bacteria Tetradecanoylphorbol Acetate Rabbits Protein Kinases Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 206(1) |
| ISSN: | 0006-291X |
| Popis: | Dystrophin is phosphorylated by several protein kinases. In this work, we have studied the effects of dystrophin phosphorylation on the binding to actin. Purified dystrophin was phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase (PKA), casein kinase II (CK-II), and protein kinase c (PKC). The results demonstrate that phosphorylation of dystrophin by PKA phosphorylation caused a three fold increase in dystrophin binding to actin. In contrast, phosphorylation by CK-II or PKC inhibited the binding to actin. These results indicate that phosphorylation of dystrophin modulates its interaction with the actin cytoskeleton. It is suggested that phosphorylation may be one mechanism for regulating protein turnover in muscle membrane-skeleton. |
| Databáze: | OpenAIRE |
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