Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin

Cell. 1990 Sep 21;62(6):1063-71. doi: 10.1016/0092-8674(90)90384-q.


As cells enter mitosis, the intermediate filament (IF) networks of interphase BHK-21 cells are depolymerized to form cytoplasmic aggregates of disassembled IFs, and the constituent IF proteins, vimentin and desmin are hyperphosphorylated at several specific sites. We have characterized one of two endogenous vimentin kinases from a particulate fraction of mitotic cell lysates. Through several purification steps, vimentin kinase activity copurifies with histone H1 kinase and both activities bind to p13suc1-Sepharose. The final enriched kinase preparation consists primarily of p34cdc2 and polypeptides of 65 and 110 kd. The purified kinase complex phosphorylates vimentin in vitro at a subset of sites phosphorylated in vivo during mitosis. Furthermore, phosphorylation of in vitro polymerized vimentin IFs by the purified kinase causes their disassembly. Therefore, vimentin is a substrate of p34cdc2 and phosphorylation of vimentin contributes to M phase reorganization of the IF network.

Publication types

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

MeSH terms

  • Animals
  • CDC2 Protein Kinase
  • Cell Line
  • Chromatography
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Cytoskeleton / ultrastructure*
  • Durapatite
  • Hydroxyapatites
  • Intermediate Filaments / ultrastructure*
  • Kinetics
  • Mitosis*
  • Phosphoproteins / isolation & purification
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Kinases / isolation & purification
  • Protein Kinases / metabolism*
  • Vimentin / metabolism*


  • Hydroxyapatites
  • Phosphoproteins
  • Vimentin
  • Durapatite
  • Protein Kinases
  • CDC2 Protein Kinase