Ca2(+)-calmodulin-dependent protein kinase II phosphorylates various types of non-epithelial intermediate filament proteins

Biochem Biophys Res Commun. 1990 Jun 29;169(3):896-904. doi: 10.1016/0006-291x(90)91977-z.

Abstract

We have investigated the actions of Ca2(+)-calmodulin (CaM)-dependent protein kinase II on various types of non-epithelial intermediate filament proteins, vimentin, desmin, glial fibrillary acidic protein (GFAP) and neurofilament triplet proteins. Most of these filament proteins could serve as substrates. The effects of phosphorylation on the filamentous structure of vimentin were investigated in sedimentation experiments and by using electron microscopy. The amount of unassembled vimentin increased linearly with increased phosphorylation. However, the extent of the effect of phosphorylation on the potential to polymerize was also affected by the MgCl2 concentration, under conditions for reassembly. The actions of Ca2(+)-CaM-dependent protein kinase II on non-epithelial intermediate filaments under physiological conditions are given attention.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain / enzymology
  • Calmodulin / physiology*
  • Desmin / metabolism
  • Glial Fibrillary Acidic Protein / metabolism
  • In Vitro Techniques
  • Intermediate Filament Proteins / metabolism*
  • Intermediate Filaments / metabolism
  • Intermediate Filaments / ultrastructure
  • Magnesium Chloride / pharmacology
  • Microscopy, Electron
  • Molecular Weight
  • Neurofilament Proteins
  • Protein Binding
  • Protein Kinases / metabolism*
  • Rats
  • Vimentin / metabolism

Substances

  • Calmodulin
  • Desmin
  • Glial Fibrillary Acidic Protein
  • Intermediate Filament Proteins
  • Neurofilament Proteins
  • Vimentin
  • Magnesium Chloride
  • Protein Kinases