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DC Field | Value | Language |
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dc.contributor.author | Baro, Barbara | - |
dc.contributor.author | Játiva, Soraya | - |
dc.contributor.author | Calabria, Inés | - |
dc.contributor.author | Vinaixa, Judith | - |
dc.contributor.author | Bech-Serra, Joan J. | - |
dc.contributor.author | Torre Gómez, Carolina de la | - |
dc.contributor.author | Rodrigues, João | - |
dc.contributor.author | Hernáez, María Luisa | - |
dc.contributor.author | Gil, Concha | - |
dc.contributor.author | Barceló-Batllori, Sílvia | - |
dc.contributor.author | Larsen, Martin R. | - |
dc.contributor.author | Queralt Badia, Ethel | - |
dc.date.accessioned | 2020-11-20T10:56:17Z | - |
dc.date.available | 2020-11-20T10:56:17Z | - |
dc.date.issued | 2018-01-24 | - |
dc.identifier.uri | http://hdl.handle.net/2445/172248 | - |
dc.description.abstract | Background: Protein phosphatase 2A (PP2A) is a family of conserved serine/threonine phosphatases involved in several essential aspects of cell growth and proliferation. PP2A(Cdc55) phosphatase has been extensively related to cell cycle events in budding yeast; however, few PP2A(Cdc55) substrates have been identified. Here, we performed a quantitative mass spectrometry approach to reveal new substrates of PP2A(Cdc55) phosphatase and new PP2A-related processes in mitotic arrested cells. Results: We identified 62 statistically significant PP2A(Cdc55) substrates involved mainly in actin-cytoskeleton organization. In addition, we validated new PP2A(Cdc55) 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. Conclusions: We used phosphoproteomics of Cdc55-deficient cells to uncover new PP2A(Cdc55) substrates 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 PP2A(Cdc55) counteracts and regulates other kinases distinct from Cdk1. Indeed, Pkc1 emerged as a novel node of PP2A(Cdc55) regulation, highlighting a major role of PP2A(Cdc55) in actin cytoskeleton and cytokinesis, gene ontology terms significantly enriched in the PP2A(Cdc55)-dependent phosphoproteome. | - |
dc.format.extent | 18 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Oxford University Press | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1093/gigascience/giy047 | - |
dc.relation.ispartof | Gigascience, 2018, vol. 7, num. 5 | - |
dc.relation.uri | https://doi.org/10.1093/gigascience/giy047 | - |
dc.rights | cc by (c) Baro et al., 2018 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | - |
dc.source | Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL)) | - |
dc.subject.classification | Mitosi | - |
dc.subject.classification | Proteïna-tirosina-fosfatasa | - |
dc.subject.other | Mitosis | - |
dc.subject.other | Protein-tyrosine phosphatase | - |
dc.title | SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.date.updated | 2020-11-11T17:47:36Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 29688323 | - |
Appears in Collections: | Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL)) |
This item is licensed under a Creative Commons License