Evidence map›Paper›PMID 25527407›Full record

ArticleEMBO reports2015

Ubiquitin acetylation inhibits polyubiquitin chain elongation.

Fumiaki Ohtake, Yasushi Saeki, Kensaku Sakamoto, Kazumasa Ohtake, Hiroyuki Nishikawa, Hikaru Tsuchiya, Tomohiko Ohta, Keiji Tanaka, Jun Kanno

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

81 citing papers in PubMed, 147 citations in OpenAlex.

  1. Review
  2. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
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  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Reading and Writing the Ubiquitin Code Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024
    Review
  15. Article
  16. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  17. Review
  18. Review
  19. Review
  20. Article

21 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

9 authors at 3 institutions in 1 country.

Fumiaki OhtakeDivision of Cellular and Molecular Toxicology, Biological Safety Research Center, National Institute of Health Sciences, Setagaya-ku Tokyo, Japan ohtake@nihs.go.jp.
Yasushi SaekiLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Sciences, Setagaya-ku Tokyo, Japan.
Kensaku SakamotoDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Tsurumi Yokohama, Japan.
Kazumasa OhtakeDivision of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Tsurumi Yokohama, Japan.
Hiroyuki NishikawaInstitute of Advanced Medical Science, St. Marianna University Graduate School of Medicine, Kawasaki, Japan.
Hikaru TsuchiyaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Sciences, Setagaya-ku Tokyo, Japan.
Tomohiko OhtaDepartment of Translational Oncology, St. Marianna University Graduate School of Medicine, Kawasaki, Japan.
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Sciences, Setagaya-ku Tokyo, Japan.
Jun KannoDivision of Cellular and Molecular Toxicology, Biological Safety Research Center, National Institute of Health Sciences, Setagaya-ku Tokyo, Japan.
Tokyo Metropolitan Institute of Medical Science · JPNational Institute of Health Sciences · JPSt. Marianna University School of Medicine · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitylation is a versatile post-translational modification (PTM). The diversity of ubiquitylation topologies, which encompasses different chain lengths and linkages, underlies its widespread cellular roles. Here, we show that endogenous ubiquitin is acetylated at lysine (K)-6 (AcK6) or K48. Acetylated ubiquitin does not affect substrate monoubiquitylation, but inhibits K11-, K48-, and K63-linked polyubiquitin chain elongation by several E2 enzymes in vitro. In cells, AcK6-mimetic ubiquitin stabilizes the monoubiquitylation of histone H2B-which we identify as an endogenous substrate of acetylated ubiquitin-and of artificial ubiquitin fusion degradation substrates. These results characterize a mechanism whereby ubiquitin, itself a PTM, is subject to another PTM to modulate mono- and polyubiquitylation, thus adding a new regulatory layer to ubiquitin biology.

Indexed as

AcetylationHumansPolyubiquitinProtein Processing, Post-TranslationalUbiquitinUbiquitinationPolyubiquitinUbiquitinacetylationmechanismpost‐translational modificationubiquitin

Identifiers

PMID25527407
PMCPMC4328746
OpenAlexW2013068694

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.