Phosphorylation of smooth muscle caldesmon by three protein kinases: Implication for domain mapping

FEBS Letters

Gusev, Nikolai B.¹  Vorotnikov, Aleksander V.¹  Shirinsky, Vladimir P.² 

[1] Department of Biochemistry, School of Biology, Moscow State University, Moscow 119899 USSR;Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, USSR Cardiology Research Center, Moscow 121552, USSR

关键词: Caldesmon;    Calmodulin;    Protein kinase;    Phosphorylation;    (Duck gizzard);   

DOI  :  10.1016/0014-5793(88)80047-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorylation of duck gizzard caldesmon by Ca²⁺/phospholipid-dependent protein kinase, Ca²⁺/calmodulin-dependent protein kinase and casein kinase II has been investigated. The Ca²⁺/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 Ca²⁺/calmodulin-dependent protein kinase phosphorylates two sites located in the N- and C-terminal domains of caldesmon.

【 授权许可】

Unknown