Evidence map›Paper›PMID 30779731›Full record

ArticlePLoS genetics2019

Cul4-Ddb1 ubiquitin ligases facilitate DNA replication-coupled sister chromatid cohesion through regulation of cohesin acetyltransferase Esco2.

Haitao Sun, Jiaxin Zhang, Siyu Xin, Meiqian Jiang, Jingjing Zhang, Zhen Li, Qinhong Cao, Huiqiang Lou

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

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  13. Esco2 and cohesin regulate CRL4 ubiquitin ligaseCell cycle (Georgetown, Tex.) · 2022
    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

8 authors at 1 institution in 1 country.

Haitao SunBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.
Jiaxin ZhangBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.
Siyu XinBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.
Meiqian JiangBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.
Jingjing ZhangBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.
Zhen LiBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.ORCID 0000-0002-4798-4161
Qinhong CaoBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.ORCID 0000-0002-2055-3513
Huiqiang LouBeijing Advanced Innovation Center for Food Nutrition and Human Health and State Key Laboratory of Agro-Biotechnology, College of Biological Sciences, China Agricultural University, Beijing, China.ORCID 0000-0003-4465-6186
China Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cohesin acetyltransferases ESCO1 and ESCO2 play a vital role in establishing sister chromatid cohesion. How ESCO1 and ESCO2 are controlled in a DNA replication-coupled manner remains unclear in higher eukaryotes. Here we show a critical role of CUL4-RING ligases (CRL4s) in cohesion establishment via regulating ESCO2 in human cells. Depletion of CUL4A, CUL4B or DDB1 subunits substantially reduces the normal cohesion efficiency. We also show that MMS22L, a vertebrate ortholog of yeast Mms22, is one of DDB1 and CUL4-associated factors (DCAFs) involved in cohesion. Several lines of evidence show selective interaction of CRL4s with ESCO2 through LxG motif, which is lost in ESCO1. Depletion of either CRL4s or ESCO2 causes a defect in SMC3 acetylation, which can be rescued by HDAC8 inhibition. More importantly, both CRL4s and PCNA act as mediators for efficiently stabilizing ESCO2 on chromatin and catalyzing SMC3 acetylation. Taken together, we propose an evolutionarily conserved mechanism in which CRL4s and PCNA promote ESCO2-dependent establishment of sister chromatid cohesion.

Indexed as

AcetylationAcetyltransferasesCell Cycle ProteinsCell LineChromatidsChromatinChromosomal Proteins, Non-HistoneCohesinsCullin ProteinsDNA-Binding ProteinsDNA ReplicationHEK293 CellsHumansNuclear ProteinsUbiquitinAcetyltransferasesCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCohesinsCUL4A protein, humanCUL4B protein, humanCullin ProteinsDDB1 protein, humanDNA-Binding ProteinsESCO2 protein, humanNuclear ProteinsUbiquitin

Identifiers

PMID30779731
PMCPMC6396947
OpenAlexW2892223599

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.