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Published August 29, 2019 | Version v2
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A Compendium to the Phosphoregulation of Mitosis

  • 1. ANZAC Research Institute, University of Sydney, Sydney, NSW 2139, Australia
  • 2. Garvan Institute of Medical Research, Sydney NSW 2010, Australia
  • 3. University of Sydney, Children's Medical Research Institute,
  • 4. Spanish National Cancer Research Centre (CNIO),

Description

The regulation of mitosis is a complex, highly ordered process involving thousands of phosphorylation and dephosphorylation events. Many details about the process are still unknown, however current estimates from large-scale, deep phospho-proteomics analysis suggest that the majority of the proteome gets fully-phosphorylated during mitosis (Olsen et al., 2010). To help in understanding how mitosis is regulated, we selected 88 phospho-events believed to play key roles, and used them to create a tailored visualization (Burgess et al., 2017) based on the ‘Minardo’ layout, in which time is represented as flowing around a schematic ‘circtanglar’ cell (Ma et al., 2013). The visualization provides a quick yet comprehensive overview of the events regulating entry, progression and exit from mitosis (Burgess et al., 2017). Each phospho-event is visually linked to its corresponding kinase or phosphatase, adding an additional layer of information. An interactive version is also available (http://www.cell.com/cell/enhanced/odonoghue2);here, users can click on each phosphosite to open up a popup that contains a brief description of the event, as well as links to supporting literature in PubMed, related 3D structures in Aquaria (O’Donoghue et al., 2015),  and protein sequence information in UniProt (The UniProt Consortium, 2019). Below, in this publication, we have compiled all the text from the 88 popups in the online interactive visualization, with the aim of making this information more easily accessible, as well as acknowledging the contributions of the >200 scientific publications that we used in assembling the visualization. This provides a comprehensive compendium of the major phospho-events currently believed to be essential for mitosis.

Notes

This compendium accompanies the publication in Cell (2017) 169:1358–1358.e1 doi: 10.1016/j.cell.2017.06.003 and the interactive website which can be found here: https://minardo.org/mitosis. In addition, the complementary S-Phase snapshot can be found here: https://minardo.org/s-phase and the associated compendium here: https://doi.org/10.5281/zenodo.3358293 A.B. is supported by CINSW FRL (ID#10/FRL/3-02), The Patricia Helen Guest Fellowship and a NBCF IIRS grant (#IIRS-18-103). S.R. is an Australian Government RTP Scholarship. M.M. is supported by MINECO (SAF2015-69920-R, ERDF-EU, and BFU2014-52125-REDT grants). J.V. and S.I.O'D. are supported by CSIRO's OCE Science Leader programme. The authors thank Benedetta Frida Baldi and Christopher Hammang for creative input.

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Related works

Is supplement to
10.1016/j.cell.2017.06.003 (DOI)

References

  • Burgess A, Vuong J, Rogers S, Malumbres M, O'Donoghue SI. SnapShot: Phosphoregulation of Mitosis. Cell (2017) 169:1358–1358.e1
  • Ma DKG, Stolte C, Kaur S, Bain M, O'Donoghue SI 2013. Visual analytics of phosphorylation time-series data on insulin response. in (AIP), 185–196. doi:10.1063/1.4825010
  • Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M 2010. Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Science Signaling. Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475.
  • O'Donoghue SI, Sabir KS, Kalemanov M, Stolte C, Wellmann B, Ho V, Roos M, Perdigão N, Buske FA, Heinrich J, Rost B, Schafferhans A 2015. Aquaria: simplifying discovery and insight from protein structures. Nature Methods. Feb;12(2):98-9. doi: 10.1038/nmeth.3258.
  • UniProt Consortium 2019. UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. Jan 8;47(D1):D506-D515. doi: 10.1093/nar/gky1049.