Evidence map›Paper›PMID 26715668›Full record

ArticleGenetics2016

Redundant Regulation of Cdk1 Tyrosine Dephosphorylation in Saccharomyces cerevisiae.

Erin K Kennedy, Michael Dysart, Noel Lianga, Elizabeth C Williams, Sophie Pilon, Carole Doré, Jean-Sebastien Deneault, Adam D Rudner

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Erin K KennedyOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada.
Michael DysartOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada.
Noel LiangaOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada.
Elizabeth C WilliamsOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada.
Sophie PilonOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada.
Carole DoréOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada Ottawa Hospital Research Institute, The Ottawa Hospital, Ottawa, ON K1H 8L6, Canada.
Jean-Sebastien DeneaultOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada.
Adam D RudnerOttawa Institute of Systems Biology and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, ON K1H 8M5, Canada arudner@uottawa.ca.ORCID http://orcid.org/0000-0002-0301-1042
University of Ottawa · CAOttawa Hospital Research Institute

Funding

Canadian Institutes of Health Research 177774
6 · The paper itself

Abstract

Cdk1 activity drives both mitotic entry and the metaphase-to-anaphase transition in all eukaryotes. The kinase Wee1 and the phosphatase Cdc25 regulate the mitotic activity of Cdk1 by the reversible phosphorylation of a conserved tyrosine residue. Mutation of cdc25 in Schizosaccharomyces pombe blocks Cdk1 dephosphorylation and causes cell cycle arrest. In contrast, deletion of MIH1, the cdc25 homolog in Saccharomyces cerevisiae, is viable. Although Cdk1-Y19 phosphorylation is elevated during mitosis in mih1∆ cells, Cdk1 is dephosphorylated as cells progress into G1, suggesting that additional phosphatases regulate Cdk1 dephosphorylation. Here we show that the phosphatase Ptp1 also regulates Cdk1 dephosphorylation in vivo and can directly dephosphorylate Cdk1 in vitro. Using a novel in vivo phosphatase assay, we also show that PP2A bound to Rts1, the budding yeast B56-regulatory subunit, regulates dephosphorylation of Cdk1 independently of a function regulating Swe1, Mih1, or Ptp1, suggesting that PP2A(Rts1) either directly dephosphorylates Cdk1-Y19 or regulates an unidentified phosphatase.

Indexed as

CDC2 Protein KinasePhosphorylationProtein Phosphatase 2Protein Tyrosine Phosphatasesras-GRF1Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTyrosineCDC25 protein, S cerevisiaeCDC2 Protein KinaseProtein Phosphatase 2Protein Tyrosine Phosphatasesras-GRF1Rts1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTyrosineCdc25/Mih1Cdk1mitosisPP2AWee1/Swe1

Identifiers

PMID26715668
PMCPMC4788127
OpenAlexW2209653733

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.