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Reference - PMID:2682257 - Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis.

Reference summary

PubMed ID
PMID:2682257
Title
Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis.
Authors
Gould KL, Nurse P
Citation
Nature 1989 Nov 02;342(6245):39-45
Publication year
1989
Abstract
The cdc2+ protein kinase (pp34) is found to be phosphorylated on tyrosine as well as serine and threonine residues in exponentially growing Schizosaccharomyces pombe. At mitosis, the level of pp34 phosphorylation on both threonine and tyrosine residues decreases. The single detectable site of tyrosine phosphorylation in pp34 has been mapped to Tyr 15, a residue within the presumptive ATP-binding domain. Substitution of this tyrosine by phenylalanine advances cells prematurely into mitosis, establishing that tyrosine phosphorylation/dephosphorylation directly regulates pp34 function.

Annotation

GO cellular component

GO:0000307 - cyclin-dependent protein kinase holoenzyme complex

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Modification

MOD:00048 - O4'-phospho-L-tyrosine

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Single locus phenotype

FYPO:0000670 - abnormal mitotic sister chromatid separation

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FYPO:0002033 - abolished protein phosphorylation during vegetative growth

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FYPO:0001052 - cut, small cell

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FYPO:0001355 - decreased vegetative cell population growth

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FYPO:0000776 - normal protein phosphorylation during vegetative growth

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FYPO:0002085 - normal vegetative cell growth

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FYPO:0002342 - septated vegetative cell

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FYPO:0006822 - viable small vegetative cell with normal cell growth rate

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