Phosphorylation of smooth muscle caldesmon by three protein kinases: implication for domain mapping.
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.
Vorotnikov
A V
AV
Department of Biochemistry, School of Biology, Moscow State University, USSR.
Shirinsky
V P
VP
Gusev
N B
NB
D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D047388:Casein Kinases; D004372:Ducks; D005895:Gizzard, Avian; D009130:Muscle, Smooth / Q000378:metabolism; D010449:Peptide Mapping; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D011494:Protein Kinases; D047388:Casein Kinases; D011493:Protein Kinase C