Help Login Create account

Data released on April 20, 2018

Supporting data for "SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast."

Baro, B; Jativa, S; Calabria, I; Vinaixa, J; Bech-Serra, J; deLaTorre, C; Rodrigues, J; Hernaez, M, L; Gil, C; Barcelo-Batllori, S; Larsen, M, R; Queralt, E (2018): Supporting data for "SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast." GigaScience Database. http://dx.doi.org/10.5524/100432 RIS BibTeX Text

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 62 statistically significant PP2ACdc55 substrates involved mainly in actincytoskeleton organization. In addition, we validated new PP2ACdc55 substrates such as Slk19 and Lte1, involved in early and late anaphase pathways, and Zeo1, a component of the cell wall integrity pathway. Finally, we constructed 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. We used phosphoproteomics of Cdc55 deficient cells to uncover new PP2ACdc55substrates and functions in mitosis. 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 distinct from Cdk1. Indeed, Pkc1 emerged as a novel node of PP2ACdc55 regulation, highlighting a major role of PP2ACdc55 in actin cytoskeleton and cytokinesis, gene ontology terms significantly enriched in the PP2ACdc55- dependent phosphoproteome.

Contact Submitter

Accessions (data included in GigaDB):

PRIDE: PXD007613

Keywords:

phosphoproteomics silac mitosis mass spectrometry 

Proteomic

http://gigadb.org/images/data/cropped/100432.jpg

Funding:

  • Funding body - Spanish Ministry of Science and Innovation
  • Award ID - BFU2011-27568
  • Comment - Plan Nacional
  • Awardee - Ethel Queralt
  • Funding body - Spanish Ministry of Economy and Competitively
  • Award ID - BFU2013-43132-P
  • Comment - Plan Nacional
  • Awardee - Ethel Queralt
  • Funding body - Spanish Ministry of Economy and Competitively
  • Award ID - BFU2016-77975-R AEI/FEDER
  • Comment - Plan Nacional
  • Awardee - Ethel Queralt
  • Funding body - Lundbeck Foundation
  • Comment - Junior Group Leader Fellowship
  • Awardee - Martin R Larsen
  • Funding body - VILLUM Foundation
  • Funding body - Spanish Ministry of Economy and Competitivity
  • Award ID - 13FIS037
  • Comment - Plan Estatal ISCIII
  • Awardee - Silvia Barcelo-Batllori
  • Funding body - Spanish Ministry of Economy and Competitivity
  • Award ID - PT13/0001/0033
  • Comment - Plan Estatal PRB2-ISCIII
  • Awardee - IDIBELL Proteomics Unit

Files: (FTP site) Table Settings

Columns:

File Description
Sample ID
Data Type
File Format
Size
Release Date
Download Link
File Attributes

File NameSample IDData TypeFile FormatSizeRelease Date 
mixed archiveTAR3.07 MB2018-03-30
ReadmeTEXT2.2 KB2018-03-30
TextTEXT8.72 KB2018-03-30
Displaying 1-3 of 3 File(s).

History:

+

Other datasets you might like: