Supporting data for "SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast."
Dataset type: Proteomic
Data released on April 20, 2018
Baro B; Jativa S; Calabria I; Vinaixa J; Bech-Serra J; deLaTorre C; Rodrigues J; Hernaez ML; Gil C; Barcelo-Batllori S; Larsen MR; 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
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.
Read the peer-reviewed publication(s):
Baro, B., Játiva, S., Calabria, I., Vinaixa, J., Bech-Serra, J.-J., de LaTorre, C., … Queralt, E. (2018). SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast. GigaScience, 7(5). doi:10.1093/gigascience/giy047
Accessions (data generated as part of this study):