Evidence map›Paper›PMID 23878248›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Pds5 promotes and protects cohesin acetylation.

Kok-Lung Chan, Thomas Gligoris, William Upcher, Yuki Kato, Katsuhiko Shirahige, Kim Nasmyth, Frédéric Beckouët

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

77 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Review
  3. 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
  4. Article
  5. Article
  6. Clinical,medRxiv : the preprint server for health sciences · 2026
    Article
  7. Article
  8. The mitotic STAG3-cohesin complex shapes male germline nucleome.Nature structural & molecular biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Cohesin organization, dynamics, and subdomain functions revealed by genetic suppressor screening.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Article
  19. Article
  20. Article

17 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

7 authors at 2 institutions in 2 countries.

Kok-Lung ChanDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Thomas Gligoris
William Upcher
Yuki Kato
Katsuhiko Shirahige
Kim Nasmyth
Frédéric Beckouët
University of Oxford · GBThe University of Tokyo · JP

Funding

Cancer Research UK 12386Medical Research CouncilWellcome Trust 091911
6 · The paper itself

Abstract

Cohesin's Smc1 and Smc3 subunits form V-shaped heterodimers, the nucleotide binding domains (NBDs) of which bind the C- and N-terminal domains, respectively, of the α-kleisin subunit, forming a large tripartite ring within in which sister DNAs are entrapped, and thereby held together (sister chromatid cohesion). During replication, establishment of stable cohesion is dependent on Eco1-mediated acetylation of Smc3's NBD, which is thought to prevent dissociation of α-kleisin from Smc3, thereby locking shut a "DNA exit gate." How Scc3 and Pds5, regulatory subunits bound to α-kleisin, regulate cohesion establishment and maintenance is poorly understood. We show here that by binding to α-kleisin adjacent to its Smc3 nucleotide binding N-terminal domain, Pds5 not only promotes cohesin's release from chromatin but also mediates de novo acetylation of Smc3 by Eco1 during S phase and subsequently prevents de-acetylation by the deacetylase Hos1/HDAC8. By first promoting cohesin's release from chromosomes and subsequently creating and guarding the chemical modification responsible for blocking release, Pds5 enables chromosomal cohesin to switch during S phase from a state of high turnover to one capable of tenaciously holding sister chromatids together for extended periods of time, a duality that has hitherto complicated analysis of this versatile cohesin subunit.

Indexed as

AcetylationAcetyltransferasesAmino Acid SequenceBinding SitesBlotting, WesternCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneChromosomes, FungalCohesinsDNA, FungalFluorescence Recovery After PhotobleachingHistone DeacetylasesLuminescent ProteinsMolecular Sequence DataMutationAcetyltransferasesCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCohesinsDNA, FungalECO1 protein, S cerevisiaeHistone DeacetylasesLuminescent ProteinsNuclear ProteinsPDS5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSMC3 protein, S cerevisiaecellgene

Identifiers

PMID23878248
PMCPMC3740900
OpenAlexW2067000276

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.