Evidence map›Paper›PMID 29688323›Full record

ArticleGigaScience2018

SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast.

Barbara Baro, Soraya Játiva, Inés Calabria, Judith Vinaixa, Joan-Josep Bech-Serra, Carolina de LaTorre, João Rodrigues, María Luisa Hernáez, Concha Gil, Silvia Barceló-Batllori and 2 more

Open access · goldAbstract read
In one paragraph

Article in GigaScience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 32 citations in OpenAlex.

  1. Decoding Cdk1 control: from mitotic thresholds to meiotic specificity.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Review
  2. Article
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  4. Article
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  11. Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024
    Article
  12. Article
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  15. Article
  16. Review
  17. Yeast Sphingolipid Phospholipase GeneMolecular and cellular biology · 2020
    Article
  18. Review
  19. Protein Phosphatases in G1 Regulation.International journal of molecular sciences · 2020
    Review
  20. PP2A Functions during Mitosis and Cytokinesis in Yeasts.International journal of molecular sciences · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 3 countries.

Barbara BaroCell Cycle Group, Cancer Epigenetics and Biology Program, Institut d'Investigacions Biomèdica de Bellvitge (IDIBELL), L'Hospitalet de Llobregat, Barcelona, Spain.
Soraya JátivaCell Cycle Group, Cancer Epigenetics and Biology Program, Institut d'Investigacions Biomèdica de Bellvitge (IDIBELL), L'Hospitalet de Llobregat, Barcelona, Spain.
Inés CalabriaCell Cycle Group, Cancer Epigenetics and Biology Program, Institut d'Investigacions Biomèdica de Bellvitge (IDIBELL), L'Hospitalet de Llobregat, Barcelona, Spain.
Judith VinaixaCell Cycle Group, Cancer Epigenetics and Biology Program, Institut d'Investigacions Biomèdica de Bellvitge (IDIBELL), L'Hospitalet de Llobregat, Barcelona, Spain.
Joan-Josep Bech-SerraIDIBELL Proteomics Unit, Institut d'Investigacions Biomèdica de Bellvitge, L'Hospitalet de Llobregat, Barcelona, Spain.
Carolina de LaTorreIDIBELL Proteomics Unit, Institut d'Investigacions Biomèdica de Bellvitge, L'Hospitalet de Llobregat, Barcelona, Spain.
João RodriguesStructural Biology Department, School of Medicine, Stanford, California, USA.
María Luisa HernáezProteomics Unit, Parque Científico de Madrid, Facultad de Farmacia, Universidad Complutense de Madrid, Madrid, Spain.
Concha GilProteomics Unit, Parque Científico de Madrid, Facultad de Farmacia, Universidad Complutense de Madrid, Madrid, Spain.
Silvia Barceló-BatlloriIDIBELL Proteomics Unit, Institut d'Investigacions Biomèdica de Bellvitge, L'Hospitalet de Llobregat, Barcelona, Spain.
Martin R LarsenDepartment of Biochemistry and Molecular Biology, Odense M, Denmark.
Ethel QueraltCell Cycle Group, Cancer Epigenetics and Biology Program, Institut d'Investigacions Biomèdica de Bellvitge (IDIBELL), L'Hospitalet de Llobregat, Barcelona, Spain.
Institut d'Investigació Biomédica de Bellvitge · ESUniversidad Complutense de Madrid · ESOdense Municipality · DKStanford Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: 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. Results: We identified 62 statistically significant PP2ACdc55 substrates involved mainly in actin-cytoskeleton 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. Conclusions: We used phosphoproteomics of Cdc55-deficient cells to uncover new PP2ACdc55 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 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.

Indexed as

Amino Acid SequenceCell Cycle ProteinsCytokinesisEndocytosisGene OntologyIsotope LabelingMetaphaseMolecular Docking SimulationPhosphoproteinsPhosphorylationProtein BindingProtein Interaction MapsProtein Phosphatase 2ProteomeProteomicsReproducibility of ResultsCDC55 protein, S cerevisiaeCell Cycle ProteinsPhosphoproteinsProtein Phosphatase 2ProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID29688323
PMCPMC5967524
OpenAlexW2801772010

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.