Evidence map›Paper›PMID 11566880›Full record

ArticleThe EMBO journal2001

Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the ubiquitin ligase APC.

M Schwab, M Neutzner, D Möcker, W Seufert

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

112 citing papers in PubMed, 209 citations in OpenAlex.

  1. WEE1 opposes APC/CNature · 2026
    Article
  2. Article
  3. Cryo-EM structures of apo-APC/C and APC/CNature communications · 2024
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  5. Article
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  10. Role of phosphorylation of Cdc20 in the regulation of the action of APC/C in mitosis.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  12. Review
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  15. Review
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  18. Review
  19. Review
  20. Article

52 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

M SchwabInstitute of Industrial Genetics, University of Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.
M Neutzner
D Möcker
W Seufert
University of Stuttgart · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-mediated proteolysis has emerged as a key mechanism of regulation in eukaryotic cells. During cell division, a multi-subunit ubiquitin ligase termed the anaphase promoting complex (APC) targets critical regulatory proteins such as securin and mitotic cyclins, and thereby triggers chromosome separation and exit from mitosis. Previous studies in the yeast Saccharomyces cerevisiae identified the conserved WD40 proteins Cdc20 and Hct1 (Cdh1) as substrate-specific activators of the APC, but their precise mechanism of action has remained unclear. This study provides evidence that Hct1 functions as a substrate receptor that recognizes target proteins and recruits them to the APC for ubiquitylation and subsequent proteolysis. By co-immunoprecipitation, we found that Hct1 interacted with the mitotic cyclins Clb2 and Clb3 and the polo-related kinase Cdc5, whereas Cdc20 interacted with the securin Pds1. Failure to interact with Hct1 resulted in stabilization of Clb2. Analysis of Hct1 derivatives identified the C-box, a motif required for APC association of Hct1 and conserved among Cdc20-related proteins. We propose that proteins of the Cdc20 family are substrate recognition subunits of the ubiquitin ligase APC.

Indexed as

Saccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesAmino Acid MotifsAmino Acid SequenceAnaphase-Promoting Complex-CyclosomeCdc20 ProteinsCdh1 ProteinsCell Cycle ProteinsCyclin BFungal ProteinsLigasesMitosisNuclear ProteinsProtein BindingProtein KinasesProtein Serine-Threonine KinasesAnaphase-Promoting Complex-CyclosomeCdc20 ProteinsCDC20 protein, S cerevisiaeCDC5 protein, S cerevisiaeCdh1 ProteinsCDH1 protein, S cerevisiaeCell Cycle ProteinsCLB2 protein, S cerevisiaeCyclin BFungal ProteinsLigasesNuclear ProteinsPDS1 protein, S cerevisiaeProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSecurinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID11566880
PMCPMC125620
OpenAlexW1990368851

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.