Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II

Biochem Biophys Res Commun. 1991 Mar 29;175(3):955-62. doi: 10.1016/0006-291x(91)91658-y.

Abstract

We identified the sites on vimentin that are phosphorylated by Ca2(+)-calmodulin-dependent protein kinase II (CaM-kinase II). Sequential analysis of the purified phosphopeptides demonstrated that the sites are -Thr-Arg-Thr-Tyr-Ser(PO4)38-Leu-Gly-Ser-Ala- and -Val-Arg-Leu-Leu-Gln-Asp-Ser(PO4)82-Val-Asp-, which are located within the amino-terminal head domain of vimentin. For Ser-82 but not Ser-38, the proposed CaM-kinase II recognition amino acid sequence (Arg-X-X-Ser/Thr) was not found. Studies with a series of synthetic peptide analogs corresponding to Ser-82 and its surrounding amino acid sequence indicate that Asp-84 acts as an essential substrate specificity determinant for the Ser-82 phosphorylation by CaM-kinase II. The CaM-kinase II recognition site may be more extensive than heretofore determined.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain / enzymology
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Kinetics
  • Molecular Sequence Data
  • Oligopeptides / chemistry
  • Phosphopeptides / chemistry
  • Phosphopeptides / isolation & purification
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Rats
  • Serine*
  • Substrate Specificity
  • Vimentin / metabolism*

Substances

  • Oligopeptides
  • Phosphopeptides
  • Vimentin
  • Serine
  • Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases