Ca2+-activated, phospholipid-dependent protein kinase catalyzes the phosphorylation of actin-binding proteins |
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Authors: | S Kawamoto H Hidaka |
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Affiliation: | Department of Pharmacology, Mie University School of Medicine Tsu 514, Japan |
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Abstract: | Chicken gizzard vinculin and filamin were found to be phosphorylated by Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C). These two actin-binding proteins serve as substrates for protein kinase C specifically in the free form, whereas they are little phosphorylated by protein kinase C in the presence of F-actin. In contrast, alpha-actinin from chicken gizzard is less susceptible to phosphorylation by protein kinase C, either in the presence or in the absence of F-actin. In light of these data, the possibility that Ca2+ and phospholipid-dependent phosphorylation by protein kinase C may modulate the function of actin-binding proteins has to be considered. |
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Keywords: | EGTA ethylene glycol bis (β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid SDS sodium dodecyl sulfate TPA 12-O-tetradecanoylphorbol-13-acetate protein kinase C phospholipid-dependent protein kinase |
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