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PXD001559

PXD001559 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGlobal phosphoproteomic mapping of early mitotic exit in human cells identifies novel substrate dephosphorylation motifs
DescriptionEntry 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.
HostingRepositoryPRIDE
AnnounceDate2017-10-24
AnnouncementXMLSubmission_2017-10-24_00:16:01.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAndrew Burgess
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListphosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentLTQ Orbitrap Velos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02014-12-02 02:01:03ID requested
12015-06-25 01:42:34announced
22017-06-21 00:30:50announcedUpdated project metadata.
32017-10-24 00:16:02announcedUpdated 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 affiliationThe 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 emaila.burgess@garvan.org.au
lab head
Andrew Burgess
contact affiliationGarvan Institute of Medical Research
contact emaila.burgess@garvan.org.au
dataset submitter
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