cdc2 phosphorylation is required for its interaction with cyclin

Ducommun, B., Brambilla, P., Felix, M. A., Franza, B. R., Karsenti, E., Draetta, G. (November 1991) cdc2 phosphorylation is required for its interaction with cyclin. Embo Journal, 10 (11). pp. 3311-3319. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/1833185

Abstract

Activation of the cdc2 protein kinase at different stages of the cell cycle is regulated by post-translational modifications and interactions with cyclins. We show that in vitro translated human cdc2 binds very poorly to A and B cyclins, unless it has been preincubated with a Xenopus egg extract. This results in the phosphorylation of cdc2 which allows binding to cyclins. The replacement of Thr161, a residue conserved and phosphorylated in other protein kinases, with valine inhibits cdc2 association with A and B cyclins. In addition, mutations in the amino-terminus of cdc2 and within the conserved 'PSTAIR'region strongly inhibit binding. The Thr161Val mutation causes a lethal phenotype in the fission yeast Schizosacharomyces pombe, while replacement of Thr161 with glutamic acid, potentially mimicking phosphorylation, causes uncoordination of mitosis and multiple cytokinesis. These results suggest that a threonine phosphorylation/dephosphorylation cycle is involved in regulating cdc2 function.

Item Type: Paper
Uncontrolled Keywords: cdc2 protein kinase cyclin phosphorylation dependent protein-kinase alanine-scanning mutagenesis cell-cycle fission yeast tyrosine phosphorylation h1 kinase activation xenopus gene dephosphorylation
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > Cyclins
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cdc2
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: November 1991
Date Deposited: 14 Jan 2016 17:52
Last Modified: 14 Jan 2016 17:52
PMCID: PMC453057
URI: http://repository.cshl.edu/id/eprint/32046

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