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

Ying Hao Chou*, James R. Bischoff, David Beach, Robert D. Goldman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

254 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1063-1071
Number of pages9
Issue number6
StatePublished - Sep 21 1990

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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