Evidence map›Paper›PMID 21467995›Full record

ArticleCell research2011

Xbp1-mediated histone H4 deacetylation contributes to DNA double-strand break repair in yeast.

Ran Tao, Hua Chen, Chan Gao, Peng Xue, Fuquan Yang, Jing-Dong J Han, Bing Zhou, Ye-Guang Chen

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Understanding the impact of ER stress on lung physiology.Frontiers in cell and developmental biology · 2024
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  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

8 authors at 5 institutions in 2 countries.

Ran TaoThe State Key Laboratory of Biomembrane and Membrane Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
Hua Chen
Chan Gao
Peng Xue
Fuquan Yang
Jing-Dong J Han
Bing Zhou
Ye-Guang Chen
Tsinghua University · CNChinese Academy of Sciences · CNInstitute of Biophysics · CNInstitute of Genetics and Developmental Biology · CNPharmaceutical Biotechnology (Czechia) · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xbp1 has been shown to regulate the cell cycle as a transcriptional repressor in budding yeast Saccharomyces cerevisiae. In this study, we demonstrated that Xbp1 regulates DNA double-strand break (DSB) repair in S. cerevisiae. Xbp1 physically and genetically interacts with the histone deacetylase Rpd3 complex. Chromatin immunoprecipitation revealed that Xbp1 is required for efficient deacetylation of histone H4 flanking DSBs by the Rpd3 complex. Deletion of XBP1 leads to the delayed deacetylation of histone H4, which is coupled with increased nucleosome displacement, increased DNA end resection and decreased non-homologous end-joining (NHEJ). In response to DNA damage, Xbp1 is upregulated in a Mec1-Rad9-Rad53 checkpoint pathway-dependent manner and undergoes dephosphorylation. Cdk1, a central regulator of S. cerevisiae cell cycle, is responsible for Xbp1 phosphorylation at residues Ser146, Ser271 and Ser551. Substitution of these serine residues with alanine not only increases the association of Xbp1 with the Rpd3 complex and its recruitment to a DSB, but also promotes DSB repair. Together, our findings reveal a role for Xbp1 in DSB repair via NHEJ through regulation of histone H4 acetylation and nucleosome displacement in a positive feedback manner.

Indexed as

DNA Breaks, Double-StrandedDNA End-Joining RepairAcetylationCDC2 Protein KinaseCell Cycle CheckpointsChromatin Assembly and DisassemblyChromatin ImmunoprecipitationHistone DeacetylasesHistonesPhosphorylationRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUp-RegulationCDC2 Protein KinaseHistone DeacetylasesHistonesRepressor ProteinsRPD3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsXBP1 protein, S cerevisiae

Identifiers

PMID21467995
PMCPMC3364731
OpenAlexW2146068125

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.