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 Schizosaccharomyces 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

Ducommun, B., Brambilla, P., Félix, M., Franza, B., Karsenti, E., Draetta, G. (1991). Cdc2 phosphorylation is required for its interaction with cyclin. EMBO JOURNAL, 10(11), 3311-3319.

Cdc2 phosphorylation is required for its interaction with cyclin

BRAMBILLA, PAOLO
Secondo
;
1991

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 Schizosaccharomyces 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
Articolo in rivista - Articolo scientifico
Amino Acid Sequence; Animals; CDC2 Protein Kinase; Cyclins; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Gene Expression; Genes, Fungal; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphorylation; Protein Biosynthesis; Schizosaccharomyces; Threonine; Transcription, Genetic; Xenopus
English
3311
3319
9
Ducommun, B., Brambilla, P., Félix, M., Franza, B., Karsenti, E., Draetta, G. (1991). Cdc2 phosphorylation is required for its interaction with cyclin. EMBO JOURNAL, 10(11), 3311-3319.
Ducommun, B; Brambilla, P; Félix, M; Franza, B; Karsenti, E; Draetta, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/162266
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