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

FEBS Lett. 1988 Aug 29;236(2):321-4. doi: 10.1016/0014-5793(88)80047-4.

Abstract

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.

MeSH terms

  • Animals
  • Binding Sites
  • Calmodulin / metabolism
  • Calmodulin-Binding Proteins / metabolism*
  • Casein Kinases
  • Ducks
  • Gizzard, Avian
  • Muscle, Smooth / metabolism
  • Peptide Mapping
  • Phosphorylation
  • Protein Kinase C / metabolism
  • Protein Kinases / metabolism*

Substances

  • Calmodulin
  • Calmodulin-Binding Proteins
  • Protein Kinases
  • Casein Kinases
  • Protein Kinase C