Evidence map›Paper›PMID 25220052›Full record

ArticleCurrent biology : CB2014

Cohesin's ATPase activity couples cohesin loading onto DNA with Smc3 acetylation.

Rene Ladurner, Venugopal Bhaskara, Pim J Huis in 't Veld, Iain F Davidson, Emanuel Kreidl, Georg Petzold, Jan-Michael Peters

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.0field-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

57 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
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  8. Cohesin organizes 3D DNA contacts surrounding active enhancers inbioRxiv : the preprint server for biology · 2024
    Article
  9. Article
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  12. Cohesin organization, dynamics, and subdomain functions revealed by genetic suppressor screening.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Article
  13. Cohesin ATPase activities regulate DNA binding and coiled-coil configuration.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Genome folding through loop extrusion by SMC complexes.Nature reviews. Molecular cell biology · 2021
    Review
  16. Article
  17. Article
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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

7 authors at 1 institution in 1 country.

Rene LadurnerResearch Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.
Venugopal BhaskaraResearch Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.
Pim J Huis in 't VeldResearch Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.
Iain F DavidsonResearch Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.
Emanuel KreidlResearch Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.
Georg PetzoldResearch Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.
Jan-Michael PetersResearch Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria. Electronic address: peters@imp.ac.at.
Research Institute of Molecular Pathology · AT

Funding

Austrian Science Fund FWF Z 196
6 · The paper itself

Abstract

backgroundCohesin mediates sister chromatid cohesion by topologically entrapping sister DNA molecules inside its ring structure. Cohesin is loaded onto DNA by the Scc2/NIPBL-Scc4/MAU2-loading complex in a manner that depends on the adenosine triphosphatase (ATPase) activity of cohesin's Smc1 and Smc3 subunits. Subsequent cohesion establishment during DNA replication depends on Smc3 acetylation by Esco1 and Esco2 and on recruitment of sororin, which "locks" cohesin on DNA by inactivating the cohesin release factor Wapl.

resultsHuman cohesin ATPase mutants associate transiently with DNA in a manner that depends on the loading complex but cannot be stabilized on chromatin by depletion of Wapl. These mutants cannot be acetylated, fail to interact with sororin, and do not mediate cohesion. The absence of Smc3 acetylation in the ATPase mutants is not a consequence of their transient association with DNA but is directly caused by their inability to hydrolyze ATP because acetylation of wild-type cohesin also depends on ATP hydrolysis.

conclusionsOur data indicate that cohesion establishment involves the following steps. First, cohesin transiently associates with DNA in a manner that depends on the loading complex. Subsequently, ATP hydrolysis by cohesin leads to entrapment of DNA and converts Smc3 into a state that can be acetylated. Finally, Smc3 acetylation leads to recruitment of sororin, inhibition of Wapl, and stabilization of cohesin on DNA. Our finding that cohesin's ATPase activity is required for both cohesin loading and Smc3 acetylation raises the possibility that cohesion establishment is directly coupled to the reaction in which cohesin entraps DNA.

Indexed as

Gene Expression RegulationAdenosine TriphosphatasesCell Cycle ProteinsChondroitin Sulfate ProteoglycansChromatinChromosomal Proteins, Non-HistoneCohesinsDNA-Binding ProteinsHumansHydrolysisIntercellular Signaling Peptides and ProteinsMutationProteinsSister Chromatid ExchangeAdenosine TriphosphatasesCell Cycle ProteinsChondroitin Sulfate ProteoglycansChromatinChromosomal Proteins, Non-HistoneCohesinsDNA-Binding ProteinsIntercellular Signaling Peptides and ProteinsMAU2 protein, humanNIPBL protein, humanProteinsSMC3 protein, human

Identifiers

PMID25220052
PMCPMC4188815
OpenAlexW2000068315

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.