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PXD012860

PXD012860 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleCdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit
DescriptionTemporal control over protein phosphorylation and dephosphorylation is crucial for accurate chromosome segregation and for completion of the cell division cycle during exit from mitosis. In budding yeast, the Cdc14 phosphatase is thought to be a major regulator at this time, while in higher eukaryotes PP2A phosphatases take a dominant role. Here, we use time-resolved phosphoproteome analysis in budding yeast to evaluate the respective contributions of Cdc14 and the two main PP2A isoforms, PP2A(Cdc55) and PP2A(Rts1). This reveals an overlapping requirement for all three phosphatases during mitotic progression. Cdc14 instructs the sequential pattern of phosphorylation changes, in part through its preferential recognition of serine-based cyclin-dependent kinase (Cdk) substrates. PP2A(Cdc55) and PP2A(Rts1) in turn exhibit a broad substrate spectrum with some selectivity for phospho-threonines and a role for PP2A(Rts1) in sustaining Aurora kinase activity. Our results illustrate synergy and coordination between phosphatases as they orchestrate phosphoproteome dynamics during mitotic progression.
HostingRepositoryPRIDE
AnnounceDate2019-11-12
AnnouncementXMLSubmission_2019-11-12_01:34:02.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAndrew Jones
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListphosphorylated residue
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-02-25 03:31:16ID requested
12019-11-12 01:34:03announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: Mitotosis, Cdc14, PP2A, Phosphatase, TMT, Orbitrap
Contact List
Bram Snijders
contact affiliationMass Spectrometry Proteomics Science Technology Platform, The Francis Crick Institute
contact emailBram.Snijders@crick.ac.uk
lab head
Andrew Jones
contact affiliationThe Francis Crick Institute
contact emailAndrew.Jones@crick.ac.uk
dataset submitter
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Dataset FTP location
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