Evidence map›Paper›PMID 23049888›Full record

ArticlePloS one2012

Identification of anaphase promoting complex substrates in S. cerevisiae.

Denis Ostapenko, Janet L Burton, Mark J Solomon

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Identification of Genes inG3 (Bethesda, Md.) · 2017
    Article
  12. Erratum to: Controlling the response to DNA damage by the APC/C-Cdh1.Cellular and molecular life sciences : CMLS · 2016
    Article
  13. Controlling the response to DNA damage by the APC/C-Cdh1.Cellular and molecular life sciences : CMLS · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Cell cycle-regulated transcription: effectively using a genomics toolbox.Methods in molecular biology (Clifton, N.J.) · 2014
    Article
  18. Article
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

3 authors at 2 institutions in 1 country.

Denis OstapenkoDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.
Janet L Burton
Mark J Solomon
Yale University · USTexas A&M University · US

Funding

Anaphase Promoting Complex-mediated ProteolysisR01GM076200 · NIGMS · YALE UNIVERSITY · PI SOLOMON, MARK J · 2006 to 2009
$1.6M
Pseudosubstrate Inhibition of the Anaphase Promoting ComplexR01GM088272 · NIGMS · YALE UNIVERSITY · PI SOLOMON, MARK J · 2009 to 2010
$662k
NIGMS NIH HHS GM76200NIGMS NIH HHS GM88272NIGMS NIH HHS R01 GM076200NIGMS NIH HHS R01 GM088272
6 · The paper itself

Abstract

The Anaphase-Promoting Complex/Cyclosome (APC/C) is an essential ubiquitin ligase that targets numerous proteins for proteasome-mediated degradation in mitosis and G1. To gain further insight into cellular pathways controlled by APC/C(Cdh1), we developed two complementary approaches to identify additional APC/C(Cdh1) substrates in budding yeast. First, we analyzed the stabilities of proteins that were expressed at the same time in the cell cycle as known APC/C substrates. Second, we screened for proteins capable of interacting with the Cdh1 substrate-binding protein in a yeast two-hybrid system. Here we characterize five potential APC/C substrates identified using these approaches: the transcription factors Tos4 and Pdr3; the mRNA processing factor Fir1; the spindle checkpoint protein kinase Mps1; and a protein of unknown function, Ybr138C. Analysis of the degradation motifs within these proteins revealed that the carboxyl-terminal KEN box and D-boxes of Tos4 are important for its interaction with Cdh1, whereas the N-terminal domain of Ybr138C is required for its instability. Functionally, we found that a stabilized form of Mps1 delayed cell division upon mild spindle disruption, and that elevated levels of Ybr138C reduced cell fitness. Interestingly, both Tos4 and Pdr3 have been implicated in the DNA damage response, whereas Mps1 regulates the spindle assembly checkpoint. Thus, the APC/C(Cdh1)-mediated degradation of these proteins may help to coordinate re-entry into the cell cycle following environmental stresses.

Indexed as

Gene Expression Regulation, FungalAnaphase-Promoting Complex-CyclosomeCdh1 ProteinsCell CycleCell ProliferationGene DeletionModels, BiologicalmRNA Cleavage and Polyadenylation FactorsProtein Serine-Threonine KinasesProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticTwo-Hybrid System TechniquesUbiquitin-Protein Ligase ComplexesAnaphase-Promoting Complex-CyclosomeCdh1 ProteinsCDH1 protein, S cerevisiaeFIR1 protein, S cerevisiaeMPS1 protein, S cerevisiaemRNA Cleavage and Polyadenylation FactorsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID23049888
PMCPMC3458821
OpenAlexW2027242068

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.