Evidence map›Paper›PMID 27872142›Full record

ArticleThe EMBO journal2016

Cohesin acetylation and Wapl-Pds5 oppositely regulate translocation of cohesin along DNA.

Mai Kanke, Eri Tahara, Pim J Huis In't Veld, Tomoko Nishiyama

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2016. 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
11.3field-weighted citation impact, top 1% 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, 149 citations in OpenAlex.

  1. Article
  2. PDS5A and TOP2B cooperate for chromatin recruitment via CTCF.bioRxiv : the preprint server for biology · 2026
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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

4 authors at 2 institutions in 2 countries.

Mai KankeDivision of Biological Science, Graduate School of Science Nagoya University, Nagoya, Japan.
Eri TaharaDivision of Biological Science, Graduate School of Science Nagoya University, Nagoya, Japan.
Pim J Huis In't VeldResearch Institute of Molecular Pathology, Vienna, Austria.
Tomoko NishiyamaDivision of Biological Science, Graduate School of Science Nagoya University, Nagoya, Japan nishiyama@bio.nagoya-u.ac.jp.ORCID 0000-0002-8349-6536
Nagoya University · JPResearch Institute of Molecular Pathology · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cohesin is a ring-shaped protein complex that plays a crucial role in sister chromatid cohesion and gene expression. The dynamic association of cohesin with chromatin is essential for these functions. However, the exact nature of cohesin dynamics, particularly cohesin translocation, remains unclear. We evaluated the dynamics of individual cohesin molecules on DNA and found that the cohesin core complex possesses an intrinsic ability to traverse DNA in an adenosine triphosphatase (ATPase)-dependent manner. Translocation ability is suppressed in the presence of Wapl-Pds5 and Sororin; this suppression is alleviated by the acetylation of cohesin and the action of mitotic kinases. In Xenopus laevis egg extracts, cohesin is translocated on unreplicated DNA in an ATPase- and Smc3 acetylation-dependent manner. Cohesin movement changes from bidirectional to unidirectional when cohesin faces DNA replication; otherwise, it is incorporated into replicating DNA without being translocated or is dissociated from replicating DNA This study provides insight into the nature of individual cohesin dynamics and the mechanisms by which cohesin achieves cohesion in different chromatin contexts.

Indexed as

MovementProtein Processing, Post-TranslationalAcetylationAdenosine TriphosphateAnimalsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNAXenopus laevisXenopus ProteinsAdenosine TriphosphateCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNAPDS5 protein, Xenopussororin, XenopusWAPL protein, XenopusXenopus Proteinschromosome segregationcohesinDNA replicationpost‐translational modificationsingle‐molecule TIRF microscopy

Identifiers

PMID27872142
PMCPMC5167340
OpenAlexW2555146308

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.