Phosphorylation of dynamin by cdc2 kinase

Biochem Biophys Res Commun. 1994 Jul 29;202(2):1127-33. doi: 10.1006/bbrc.1994.2045.

Abstract

A 100kD microtubule-bundling protein dynamin was phosphorylated in vitro by cdc2 kinase to approximately 1 mol of phosphate/mol of dynamin at a serine residue. These phosphorylations of dynamin greatly reduced its binding ability to microtubules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Brain Chemistry
  • CDC2 Protein Kinase / metabolism*
  • Dynamins
  • Electrophoresis, Polyacrylamide Gel
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / metabolism*
  • HeLa Cells / enzymology
  • Humans
  • Microscopy, Electron
  • Microtubules / metabolism
  • Phosphates / metabolism*
  • Phosphorylation
  • Phosphoserine / metabolism
  • Rats

Substances

  • Phosphates
  • Phosphoserine
  • CDC2 Protein Kinase
  • GTP Phosphohydrolases
  • Dynamins