Evidence map›Paper›PMID 28819127›Full record

ArticleScientific reports2017

Multiple E3s promote the degradation of histone H3 variant Cse4.

Haili Cheng, Xin Bao, Xin Gan, Shiwen Luo, Hai Rao

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
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  7. The Protein Response of Salt-TolerantJournal of fungi (Basel, Switzerland) · 2024
    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

5 authors at 2 institutions in 2 countries.

Haili ChengDepartment of Molecular Medicine, The University of Texas Health Science Center, San Antonio, TX, 78229, USA. chengh3@livemail.uthscsa.edu.
Xin BaoDepartment of Molecular Medicine, The University of Texas Health Science Center, San Antonio, TX, 78229, USA.
Xin GanResearch Institute of Respiratory Medicine, The First Affiliated Hospital, Nanchang University, Nanchang, China.
Shiwen LuoCenter for Experimental Medicine, The First Affiliated Hospital, Nanchang University, Nanchang, China.
Hai RaoDepartment of Molecular Medicine, The University of Texas Health Science Center, San Antonio, TX, 78229, USA. raoh@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · USFirst Affiliated Hospital of Nanchang University · CN

Funding

Institute for Integration of Medicine & Science: A Partnership to Improve HealthUL1TR001120 · NCATS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI CLARK, ROBERT A, HARGREAVES, KENNETH M · 2013 to 2017
$16.5M
How a sun protection complex moonlights in proteolysisR01GM118350 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI RAO, HAI · 2016 to 2017
$598k
NCATS NIH HHS UL1 TR001120NIGMS NIH HHS R01 GM118350
6 · The paper itself

Abstract

The histone H3-like protein Cse4/CENP-A acts as a key molecular marker that differentiates the special centromeric chromatin structures from bulk nucleosomes. As altered Cse4/CENP-A activity leads to genome instability, it is pivotal to understand the mechanism underlying Cse4 regulation. Here, we demonstrate that four ubiquitin ligases (i.e., Ubr1, Slx5, Psh1, and Rcy1) work in parallel to promote Cse4 turnover in yeast. Interestingly, Cse4 overexpression leads to cellular toxicity and cell cycle delay in yeast cells lacking PSH1, but not in cells lacking UBR1, suggesting different roles of these two degradation pathways. Our findings suggest that various ubiquitin ligases collaborate to keep the Cse4 level in check, providing a basis for further delineating the intricate network involved in Cse4 regulation.

Indexed as

Chromosomal Proteins, Non-HistoneDNA-Binding ProteinsF-Box ProteinsHistonesMutationPeptide Elongation FactorsProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesVesicular Transport ProteinsChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNA-Binding ProteinsF-Box ProteinsHistonesPeptide Elongation FactorsPsh1 protein, S cerevisiaeRCY1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSlx5 protein, S cerevisiaeUbiquitin-Protein LigasesUBR1 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID28819127
PMCPMC5561092
OpenAlexW2745079848

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.