Evidence map›Paper›PMID 22901742›Full record

ArticleCell2012

Cohesin's DNA exit gate is distinct from its entrance gate and is regulated by acetylation.

Kok-Lung Chan, Maurici B Roig, Bin Hu, Frédéric Beckouët, Jean Metson, Kim Nasmyth

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed, 1 pooled it
8.5field-weighted citation impact, top 2% 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

156 citing papers in PubMed, 1 synthesis or guideline pooled it, 281 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Cohesin acetylation and ATPase activity control cohesion and loop architecture through distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Clinical,medRxiv : the preprint server for health sciences · 2026
    Article
  12. Article
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  14. Article
  15. Article
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  17. Article
  18. Article
  19. Nucleic Acids and Electrical Signals.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  20. Article

96 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

6 authors at 1 institution in 1 country.

Kok-Lung ChanUniversity of Oxford, Department of Biochemistry, South Parks Road, Oxford OX1 3QU, UK.
Maurici B Roig
Bin Hu
Frédéric Beckouët
Jean Metson
Kim Nasmyth
University of Oxford · GB

Funding

Cancer Research UK 12386Wellcome Trust 091911
6 · The paper itself

Abstract

Sister chromatid cohesion is mediated by entrapment of sister DNAs by a tripartite ring composed of cohesin's Smc1, Smc3, and α-kleisin subunits. Cohesion requires acetylation of Smc3 by Eco1, whose role is to counteract an inhibitory (antiestablishment) activity associated with cohesin's Wapl subunit. We show that mutations abrogating antiestablishment activity also reduce turnover of cohesin on pericentric chromatin. Our results reveal a "releasing" activity inherent to cohesin complexes transiently associated with Wapl that catalyzes their dissociation from chromosomes. Fusion of Smc3's nucleotide binding domain to α-kleisin's N-terminal domain also reduces cohesin turnover within pericentric chromatin and permits establishment of Wapl-resistant cohesion in the absence of Eco1. We suggest that releasing activity opens the Smc3/α-kleisin interface, creating a DNA exit gate distinct from its proposed entry gate at the Smc1/3 interface. According to this notion, the function of Smc3 acetylation is to block its dissociation from α-kleisin. The functional implications of regulated ring opening are discussed.

Indexed as

AcetylationAcetyltransferasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneChromosomes, FungalCohesinsDNA ReplicationNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructural Maintenance of Chromosome Protein 1AcetyltransferasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsECO1 protein, S cerevisiaeNuclear ProteinsPDS5 protein, S cerevisiaeRAD61 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSMC3 protein, S cerevisiaeStructural Maintenance of Chromosome Protein 1

Identifiers

PMID22901742
PMCPMC3485559
OpenAlexW2003101935

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.