PXD012860-2

PXD012860 is an original dataset announced via ProteomeXchange.

Title	Cdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit
Description	Temporal 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.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:57:21.054.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Andrew Jones
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	phosphorylated residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2019-02-25 03:31:16	ID requested
1	2019-11-12 01:34:03	announced
⏵ 2	2024-10-22 04:57:21	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

submitter keyword: TMT, PP2A, Phosphatase, Orbitrap,Mitotosis, Cdc14

Bram Snijders
contact affiliation	Mass Spectrometry Proteomics Science Technology Platform, The Francis Crick Institute
contact email	Bram.Snijders@crick.ac.uk
lab head
Andrew Jones
contact affiliation	The Francis Crick Institute
contact email	Andrew.Jones@crick.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD012860
     1. Label: PRIDE project
     2. Name: Cdc14 and PP2A Phosphatases Cooperate to Shape Phosphoproteome Dynamics during Mitotic Exit