Phosphorylation of neurofilament proteins by endogenous calcium/calmodulin-dependent protein kinase

Biochem Biophys Res Commun. 1985 Aug 15;130(3):957-63. doi: 10.1016/0006-291x(85)91708-5.

Abstract

A protein fraction containing neurofilaments was prepared from rat brain cytosol by differential centrifugation and gel filtration chromatography. These preparations were enriched for a calcium/calmodulin-dependent kinase activity that phosphorylated endogenous neurofilament proteins. The enzyme incorporated approximately 1 mol PO4/mol of each neurofilament triplet polypeptide. These data suggest that a calmodulin-dependent kinase may mediate some of the effects of calcium on cytoskeletal function by phosphorylation of neurofilament proteins.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Brain / enzymology*
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Calmodulin / isolation & purification
  • Cattle
  • Cytosol / enzymology
  • Electrophoresis, Polyacrylamide Gel
  • Intermediate Filament Proteins / isolation & purification
  • Intermediate Filament Proteins / metabolism*
  • Kinetics
  • Molecular Weight
  • Neurofilament Proteins
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Rats
  • Spinal Cord / metabolism

Substances

  • Calmodulin
  • Intermediate Filament Proteins
  • Neurofilament Proteins
  • Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases