Identification of the site phosphorylated by casein kinase II in smooth muscle caldesmon

Alicja Wawrzynow, John H. Collins, Natalia V. Bogatcheva, Alexander V. Vorotnikov, Nikolai B. Gusev

Research output: Contribution to journalArticle

16 Scopus citations


Phosphorylation of avian gizzard caldesmon by casein kinase II was investigated. The enzyme incorporates about 1 mol of phosphate per mol of caldesmon. All sites of phosphorylation are located in short chymotryptic peptides with Mr, 25-27 kDa or in the short N-terminal peptide formed after cleavage of chicken gizzard caldesmon at Cys153. The primary structure of the tryptic peptide containing the main site of duck gizzard caldesmon phosphorylation is S-E-V-N-A-Q-N-X-V-A-E-D-E-T-K. where X is an unidentified residue. presumed to be phosphorserine. Thus, Ser73 is the main site phosphorylated by casein kinase II in avian gizzard caldesmon.

Original languageEnglish (US)
Pages (from-to)213-216
Number of pages4
JournalFEBS Letters
Issue number2
StatePublished - Sep 9 1991
Externally publishedYes


  • Caldesmon
  • Casein kinase II
  • Phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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