PXD001559 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Global phosphoproteomic mapping of early mitotic exit in human cells identifies novel substrate dephosphorylation motifs |
Description | Entry into mitosis is driven by the coordinated phosphorylation of thousands of proteins. For the cell to complete mitosis and divide into two identical daughter cells it must regulate dephosphorylation of these proteins in a highly ordered, temporal manner. There is currently a lack of a complete understanding of the phosphorylation changes that occur during the initial stages of mitotic exit in human cells. Therefore, we performed a large unbiased, global analysis to map the very first dephosphorylation events that occur as cells exit mitosis. We identified and quantified the modification of >16,000 phosphosites on >3,300 unique proteins during early mitotic exit, providing up to 8-fold greater resolution than previous studies. Only a small fraction (~10%) of phosphorylation sites were dephosphorylated during early mitotic exit and these occurred on proteins involved in critical early exit events, including organization of the mitotic spindle, the spindle assembly checkpoint, and reformation of the nuclear envelope. Surprisingly this enrichment was observed across all kinase consensus motifs, indicating that it is independent of the upstream phosphorylating kinase. Therefore, dephosphorylation of these sites is likely determined by the specificity of phosphatase/s rather than the activity of kinase/s. Dephosphorylation was significantly affected by the amino acids at and surrounding the phosphorylation site, with several unique evolutionarily conserved amino acids correlating strongly with phosphorylation status. These data provide a potential mechanism for the specificity of phosphatases, and how they co-ordinate the ordered events of mitotic exit. In summary, our results provide a global overview of the phosphorylation changes that occur during the very first stages of mitotic exit, providing novel mechanistic insight into how phosphatase/s specifically regulate this critical transition. |
HostingRepository | PRIDE |
AnnounceDate | 2017-10-24 |
AnnouncementXML | Submission_2017-10-24_00:16:01.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Andrew Burgess |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2014-12-02 02:01:03 | ID requested | |
1 | 2015-06-25 01:42:34 | announced | |
2 | 2017-06-21 00:30:50 | announced | Updated project metadata. |
⏵ 3 | 2017-10-24 00:16:02 | announced | Updated project metadata. |
Publication List
McCloy RA, Parker BL, Rogers S, Chaudhuri R, Gayevskiy V, Hoffman NJ, Ali N, Watkins DN, Daly RJ, James DE, Lorca T, Castro A, Burgess A, Global Phosphoproteomic Mapping of Early Mitotic Exit in Human Cells Identifies Novel Substrate Dephosphorylation Motifs. Mol Cell Proteomics, 14(8):2194-212(2015) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Mitosis, mitotic exit, phosphorylation, kinase, phosphatase, SILAC, phosphoproteomics, PRC1, MYC, motif, spindle assembly checkpoint. |
Contact List
Andrew Burgess |
contact affiliation | The Kinghorn Cancer Center, Garvan Institute of Medical Research, Darlinghurst, NSW, 2010, Australia. St. Vincent's Clinical School, Faculty of Medicine, UNSW, Darlinghurst, NSW, Australia |
contact email | a.burgess@garvan.org.au |
lab head | |
Andrew Burgess |
contact affiliation | Garvan Institute of Medical Research |
contact email | a.burgess@garvan.org.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD001559
- Label: PRIDE project
- Name: Global phosphoproteomic mapping of early mitotic exit in human cells identifies novel substrate dephosphorylation motifs