Phosphorylation at Thr167 is required for Schizosaccharomyces pombe p34cdc2 function.

Gould KL, Moreno S, Owen DJ, Sazer S, Nurse P
EMBO J. 1991 10 (11): 3297-309

PMID: 1655416 · PMCID: PMC453056

Eukaryotic cell cycle progression requires the periodic activation and inactivation of a protein-serine/threonine kinase which in fission yeast is encoded by the cdc2+ gene. The activity of this gene product, p34cdc2, is controlled by numerous interactions with other proteins and by its phosphorylation state. In fission yeast, p34cdc2 is phosphorylated on two sites, one of which has been identified as Tyr15. Dephosphorylation of Tyr15 regulates the initiation of mitosis. To understand more completely the regulation of p34cdc2 kinase activity, we have identified the second site of phosphorylation as Thr167, a residue conserved amongst all p34cdc2 homologues. By analysing the phenotypes of cells expressing various position 167 mutations and performing in vitro experiments, we establish that Thr167 phosphorylation is required for p34cdc2 kinase activity at mitosis and is involved in the association of p34cdc2 with cyclin B. Dephosphorylation of Thr167 might also play a role in the exit from mitosis.

MeSH Terms (13)

Amino Acid Sequence Base Sequence CDC2 Protein Kinase DNA, Fungal Flow Cytometry Genes, Fungal Molecular Sequence Data Mutation Phosphorylation Phosphotransferases Schizosaccharomyces Sequence Alignment Threonine

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