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Phosphorylation of smooth muscle caldesmon by three protein kinases: Implication for domain mapping
Author(s) -
Vorotnikov Aleksander V.,
Shirinsky Vladimir P.,
Gusev Nikolai B.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80047-4
Subject(s) - caldesmon , calmodulin , phosphorylation , kinase , casein kinase 2 , biochemistry , protein kinase a , chemistry , protein kinase c , microbiology and biotechnology , biology , mitogen activated protein kinase kinase , enzyme
Phosphorylation of duck gizzard caldesmon by Ca 2+ /phospholipid‐dependent protein kinase, Ca 2+ /calmodulin‐dependent protein kinase and casein kinase II has been investigated. The Ca 2+ /phospholipid‐dependent protein kinase incorporates more than 3 mol phosphate per mol (140 kDa) caldesmon. All phosphorylation sites are localized in the actin‐ and calmodulin‐binding peptide (40–45 kDa) supposed to be a part of the C‐terminal domain of caldesmon. Casein kinase II phosphorylates only one site located in a short (25–27 kDa) peptide, presumably in the caldesmon N‐terminal domain. The Ca 2+ /calmodulin‐dependent protein kinase phosphorylates two sites located in the N‐ and C‐terminal domains of caldesmon.