PXD004461

PXD004461 is an original dataset announced via ProteomeXchange.

Title	PP21Cdc55 phosphatase imposes phosphothreonine-specific ordering of cell cycle phosphorylation
Description	In the quantitative model for cell cycle control, progression from G1 through S phase and into mitosis is ordered by thresholds of increasing cyclin-dependent kinase (Cdk) activity. How such thresholds are read out by substrates, that respond with the correct phosphorylation timing, if not known. In budding yeast, Cdk phosphorylates its many substrates with widely varying efficiencies, but there is no obvious correlation between phosphorylation efficiency and timing. Instead, we explore here whether Cdk-counteracting phosphatases impose Cdk thresholds. We find that the abundant PP2ACdc55 phosphatase counteracts Cdk phosphorylation in interphase and delays phosphorylation of late Cdk substrates, an effect that is independent of its known impact on the Cdk tyrosine phosphorylation status. Strikingly, PP2ACdc55 specifically counteracts phosphorylation of threonine residues. Consequently, we find that threonine-directed phosphorylation occurs late in the cell cycle, compared to serine phosphorylation. Late phosphorylation of Ndd1, a model substrate, depends on threonine identity. Our results support a model in which phosphatases contribute to ordering cell cycle progression by directly counteracting Cdk phosphorylation and unveil a principle of cell cycle control based on the phosphoacceptor amino acid.
HostingRepository	PRIDE
AnnounceDate	2017-10-24
AnnouncementXML	Submission_2017-10-24_04:49:37.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; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2016-06-29 02:14:28	ID requested
1	2017-01-23 11:13:51	announced
2	2017-01-31 02:10:49	announced	Updated publication reference for PubMed record(s): 28132839.
3	2017-02-14 00:30:03	announced	Updated project metadata.
⏵ 4	2017-10-24 04:49:38	announced	Updated project metadata.

Godfrey M, Touati SA, Kataria M, Jones A, Snijders AP, Uhlmann F, Phosphatase Imposes Ordered Cell-Cycle Phosphorylation by Opposing Threonine Phosphorylation. Mol Cell, 65(3):393-402.e3(2017) [pubmed]

curator keyword: Biological

submitter keyword: SILAC, phosphorylation, phosphatase, Cdk, Cell cycle

Ambrosius Snijders
contact affiliation	Protein Analysis and Proteomics 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

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2017/01/PXD004461

PRIDE project URI

• PRIDE
  1. PXD004461
     1. Label: PRIDE project
     2. Name: PP21Cdc55 phosphatase imposes phosphothreonine-specific ordering of cell cycle phosphorylation