Rogers, S., McLoy, R. A, Parker, B. L, Chaudhuri, R., Gayevskiy, V., Hoffman, N. J, Watkins, D. N, Daly, R. J, James, D. E & Burgess, A. (2015). Dataset from the global phosphoproteomic mapping of early mitotic exit in human cells. Data in Brief,5 45-52. Netherlands: Elsevier Inc.. Retrieved from https://doi.org/10.1016/j.dib.2015.08.010
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 unique proteins, and quantified the temporal phosphorylation changes that occur during early mitotic exit ( McCloy et al., 2015 ). Furthermore, we annotated the majority of these phosphorylation sites with a high confidence upstream kinase using published, motif and prediction based methods. The results from this study have been deposited into the ProteomeXchange repository with identifier PXD001559. Here we provide additional analysis of this dataset; for each of the major mitotic kinases we identified motifs that correlated strongly with phosphorylation status. These motifs could be used to predict the stability of phosphorylated residues in proteins of interest, and help infer potential functional roles for uncharacterized phosphorylations. In addition, we provide validation at the single cell level that serine residues phosphorylated by Cdk are stable during phosphatase dependent mitotic exit. In summary, this unique dataset contains information on the temporal mitotic stability of thousands of phosphorylation sites regulated by dozens of kinases, and information on the potential preference that phosphatases have at both the protein and individual phosphosite level. The compellation of this data provides an invaluable resource for the wider research community.
Mary MacKillop Institute for Health Research
Open Access Journal Article