PXD007613

PXD007613 is an original dataset announced via ProteomeXchange.

Title	SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast.
Description	Protein phosphatase 2A (PP2A) is a family of conserved serine/threonine phosphatases involved in several essential aspects of cell growth and proliferation. PP2ACdc55 phosphatase has been extensively related to cell cycle events in budding yeast, however few PP2ACdc55 substrates have been identified. Here, we performed a quantitative mass spectrometry approach to reveal new substrates of PP2ACdc55 phosphatase and new PP2A related processes in mitotic arrested cells. We identified 626 potential PP2ACdc55 substrates involved in a broad range of mitotic processes. As expected, several hyperphosphorylated proteins corresponded to Cdk1-dependent substrates, although other kinases’ consensus motifs were also enriched in our dataset, suggesting that PP2ACdc55 counteracts and regulates other kinases different than Cdk1. Indeed, Pkc1 and Cla4 kinases emerged as novel nodes of PP2ACdc55 regulation, highlighting a major role of PP2ACdc55 in membrane trafficking and cytokinesis, gene ontology terms significantly enriched in the PP2ACdc55-dependent phosphoproteome. In addition, we validated two new PP2ACdc55 substrates involved in early and late anaphase pathways, Slk19 and Lte1; and we also validated Zeo1, and other potential substrates, through protein interaction experiments. Finally, we performed docking models of Cdc55 and its substrate Mob1. We found that the predominant interface on Cdc55 is mediated by a protruding loop consisting of residues 84-90, thus highlighting the relevance of these aminoacids for substrate interaction.
HostingRepository	PRIDE
AnnounceDate	2018-04-16
AnnouncementXML	Submission_2018-04-30_01:37:55.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Joan Josep Bech-Serra
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	phosphorylated residue; 6x(13)C labeled residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos; LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2017-08-31 02:50:28	ID requested
1	2018-04-16 02:18:46	announced
⏵ 2	2018-04-30 01:37:56	announced	Updated publication reference for PubMed record(s): 29688323.

Baro B, J, á, tiva S, Calabria I, Vinaixa J, Bech-Serra JJ, de LaTorre C, Rodrigues J, Hern, á, ez ML, Gil C, Barcel, ó, -Batllori S, Larsen MR, Queralt E, SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast. Gigascience, 7(5):(2018) [pubmed]

curator keyword: Biological

submitter keyword: PP2ACdc55 phosphatase, Pkc1, Cla4, mitotic exit network (MEN), Mob1.

Ethel Queralt
contact affiliation	Cell Cycle Group Cancer Epigenetics and Biology Program (PEBC) Bellvitge Isntitute of Biomedical Research (IDIBELL) Hospital Duran i Reynals Avinguda de la Gran Via de l'Hospitalet, 199-203 08908 - L'Hospitalet de Llobregat
contact email	equeralt@idibell.cat
lab head
Joan Josep Bech-Serra
contact affiliation	Posdoctoral Investigator -Proteomics Unit Institut d'Investigació Biomèdica de Bellvitge (IDIBELL) Hospital Duran i Reynals Avinguda de la Granvia, 199 (3th Floor) 08908 L'Hospitalet de Llobregat Barcelona - Spain
contact email	jbech@idibell.cat
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/2018/04/PXD007613

PRIDE project URI

• PRIDE
  1. PXD007613
     1. Label: PRIDE project
     2. Name: SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast.