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Mitotic phosphotyrosine network analysis reveals that tyrosine phosphorylation regulates Polo-like kinase 1 (PLK1)

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Science Signaling  13 Dec 2016:
Vol. 9, Issue 458, pp. rs14
DOI: 10.1126/scisignal.aah3525

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Tyrosine phosphorylation controls mitosis after all

The cell cycle is a carefully controlled process in which serine/threonine kinases play a large role. Abnormal progression or attenuation of cell cycling is implicated in the pathogenesis of various diseases, such as cancer, myocardial infarction, stroke, atherosclerosis, infection, inflammation, and neurodegenerative disorders. Caron et al. analyzed public databases for information about protein localization and tyrosine phosphorylation status in mitotic cells and devised a mitosis-associated tyrosine phosphorylation network. The extent of this network predicted that tyrosine-targeted phosphorylation plays a larger role in mitosis than previously appreciated. For example, in their network generated from data mining and in cultured cells, tyrosine phosphorylation decreased activation of Polo-like kinase 1 (PLK1), a serine/threonine kinase that promotes chromosome separation during anaphase and is often excessively abundant in cancers. The network provides a wealth of targets for exploration into cell cycle control in physiology and disease.

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