Evidence map›Paper›PMID 31000734›Full record

ArticleScientific reports2019

Proteins that physically interact with the phosphatase Cdc14 in Candida albicans have diverse roles in the cell cycle.

Iliyana N Kaneva, Ian M Sudbery, Mark J Dickman, Peter E Sudbery

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control.International journal of molecular sciences · 2020
    Review
  8. Article
  9. Review
  10. Protein-Protein Interactions inFrontiers in microbiology · 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

4 authors.

Iliyana N KanevaChELSI Institute, Department of Chemical and Biological Engineering, University of Sheffield, Sheffield, S1 3JD, UK.
Ian M SudberyDepartment of Molecular Biology and Biotechnology, University of Sheffield, S10 2TN, Sheffield, UK.
Mark J DickmanChELSI Institute, Department of Chemical and Biological Engineering, University of Sheffield, Sheffield, S1 3JD, UK. M.Dickman@shef.ac.uk.
Peter E SudberyDepartment of Molecular Biology and Biotechnology, University of Sheffield, S10 2TN, Sheffield, UK. P.Sudbery@Shef.ac.uk.

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/J002305/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/J014443/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/M012166/1
6 · The paper itself

Abstract

The chromosome complement of the human fungal pathogen Candida albicans is unusually unstable, suggesting that the process of nuclear division is error prone. The Cdc14 phosphatase plays a key role in organising the intricate choreography of mitosis and cell division. In order to understand the role of Cdc14 in C. albicans we used quantitative proteomics to identify proteins that physically interact with Cdc14. To distinguish genuine Cdc14-interactors from proteins that bound non-specifically to the affinity matrix, we used a substrate trapping mutant combined with mass spectrometry analysis using Stable Isotope Labelling with Amino Acids in Cell Culture (SILAC). The results identified 126 proteins that interact with Cdc14 of which 80% have not previously been identified as Cdc14 interactors in C. albicans or S. cerevisiae. In this set, 55 proteins are known from previous research in S. cerevisiae and S. pombe to play roles in the cell cycle, regulating the attachment of the mitotic spindle to kinetochores, mitotic exit, cytokinesis, licensing of DNA replication by re-activating pre-replication complexes, and DNA repair. Five Cdc14-interacting proteins with previously unknown functions localised to the Spindle Pole Bodies (SPBs). Thus, we have greatly increased the number of proteins that physically interact with Cdc14 in C. albicans.

Indexed as

Candida albicansCDC2 Protein KinaseCell CycleCell Cycle ProteinsFungal ProteinsIsotope LabelingMass SpectrometryMutationPhosphoprotein PhosphatasesProtein Interaction MapsProtein Tyrosine PhosphatasesSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsCDC14 protein, S cerevisiaeCDC14 protein, S pombeCDC2 Protein KinaseCell Cycle ProteinsFungal ProteinsPhosphoprotein PhosphatasesProtein Tyrosine PhosphatasesSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID31000734
PMCPMC6472416

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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.