Intermediate Filament Reorganization during Mitosis Is Mediated by P34cdc2 Phosphorylation of Vimentin

Chou, Y. H., Bischoff, J. R., Beach, D., Goldman, R. D. (September 1990) Intermediate Filament Reorganization during Mitosis Is Mediated by P34cdc2 Phosphorylation of Vimentin. Cell, 62 (6). pp. 1063-1071. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/2169348
DOI: 10.1016/0092-8674(90)90384-Q

Abstract

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.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cdc2
organs, tissues, organelles, cell types and functions > organelles, types and functions > mitosis
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
CSHL Authors:
Communities: CSHL labs > Beach lab
Depositing User: Matt Covey
Date: 21 September 1990
Date Deposited: 29 Mar 2016 16:20
Last Modified: 29 Mar 2016 16:20
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32302

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