Journal article

Dataset from the global phosphoproteomic mapping of early mitotic exit in human cells

Samuel Rogers, Rachael A McCloy, Benjamin L Parker, Rima Chaudhuri, Velimir Gayevskiy, Nolan J Hoffman, D Neil Watkins, Roger J Daly, David E James, Andrew Burgess



The presence or absence of a phosphorylation on a substrate at any particular point in time is a functional readout of the balance in activity between the regulatory kinase and the counteracting phosphatase. Understanding how stable or short-lived a phosphorylation site is required for fully appreciating the biological consequences of the phosphorylation. Our current understanding of kinases and their substrates is well established; however, the role phosphatases play is less understood. Therefore, we utilized a phosphatase dependent model of mitotic exit to identify potential substrates that are preferentially dephosphorylated. Using this method, we identified >16,000 phosphosites on >3300 ..

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University of Melbourne Researchers


Awarded by Cancer Institute NSW FRL fellowship

Funding Acknowledgements

We thank Gillian Lehrbach (Tissue Culture), Will Hughes (Microscopy) Sean J. Humphrey, Daniel J. Fazakerley and Mark Cowley for assistance. We thank the PRIDE Team at the ProteomeXchange Consortium. This work was supported by the Cancer Institute NSW FRL fellowship ID10/FRL/3-02, The Patricia Helen Guest Fellowship, and the Petre Foundation. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.