Evidence map›Paper›PMID 26975376›Full record

ArticleThe Journal of biological chemistry2016

The F-box Protein Rcy1 Is Involved in the Degradation of Histone H3 Variant Cse4 and Genome Maintenance.

Haili Cheng, Xin Bao, Hai Rao

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  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
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
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  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Conformational flexibility of histone variant CENP-AThe Journal of biological chemistry · 2018
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article
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

3 authors.

Haili ChengFrom the Department of Molecular Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229.
Xin BaoFrom the Department of Molecular Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229.
Hai RaoFrom the Department of Molecular Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229 raoh@uthscsa.edu.

Funding

Targeting ubiquitylated proteins to the proteasomeR01GM078085 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI RAO, HAI · 2007 to 2011
$1.3M
NIGMS NIH HHS R01 GM078085
6 · The paper itself

Abstract

Cse4, a histone H3-like centromeric protein, plays critical functions in chromosome segregation. Cse4 level is tightly regulated, but the underlying mechanism remains poorly understood. We employed a toxicity-based screen to look for the degradation components involved in Cse4 regulation. Here, we show that the F-box containing protein Rcy1 is required for efficient Cse4 turnover as Cse4 degradation is compromised in yeast cells lacking RCY1 Excessive Cse4 accumulation in rcy1Δ cells leads to growth retardation. Furthermore, the deletion of RCY1 is tied to enhanced chromosome instability and temperature-sensitive cell growth. Our results reveal the involvement of Rcy1 in chromosome regulation and another regulatory pathway controlling the Cse4 level and activity.

Indexed as

ProteolysisChromosomal Proteins, Non-HistoneDNA-Binding ProteinsF-Box ProteinsGenome, FungalGenomic InstabilityHistonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNA-Binding ProteinsF-Box ProteinsHistonesRCY1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport Proteinscentromereproteasomeprotein degradationubiquitinubiquitin ligase

Identifiers

PMID26975376
PMCPMC4858983

What OpenQuestion holds

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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.