Evidence map›Paper›PMID 26187467›Full record

ReviewThe Journal of biological chemistry2015

Regulating the Regulators: Recent Revelations in the Control of E3 Ubiquitin Ligases.

Vinayak Vittal, Mikaela D Stewart, Peter S Brzovic, Rachel E Klevit

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Review
  2. A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Tsg101 mimicry of canonical E2 enzymes underlies its role in ubiquitin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  14. Article
  15. Article
  16. Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Review
  18. Ubiquitin ligases: guardians of mammalian development.Nature reviews. Molecular cell biology · 2022
    Review
  19. Article
  20. Review
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

4 authors.

Vinayak VittalFrom the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742.
Mikaela D StewartFrom the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742.
Peter S BrzovicFrom the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742.
Rachel E KlevitFrom the Department of Biochemistry, University of Washington, Seattle, Washington 98195-7742 klevit@uw.edu.ORCID http://orcid.org/0000-0002-3476-969X

Funding

Interdisciplinary Tranining in Cancer ResearchT32CA080416 · NCI · UNIVERSITY OF WASHINGTON · PI STODDARD, BARRY L. · 1998 to 2023
$9.7M
Structural and Functional Characterization of BRCA1/BARD1R01GM088055 · NIGMS · UNIVERSITY OF WASHINGTON · PI KLEVIT, RACHEL E · 2009 to 2020
$6.5M
Unconventional Interactions of Human Ubiquitin Conjugating EnzymesR01GM098503 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRZOVIC, PETER S · 2012 to 2016
$1.5M
NCI NIH HHS T32 CA080416NIGMS NIH HHS R01 GM088055NIGMS NIH HHS R01 GM098503
6 · The paper itself

Abstract

Since its discovery as a post-translational signal for protein degradation, our understanding of ubiquitin (Ub) has vastly evolved. Today, we recognize that the role of Ub signaling is expansive and encompasses diverse processes including cell division, the DNA damage response, cellular immune signaling, and even organismal development. With such a wide range of functions comes a wide range of regulatory mechanisms that control the activity of the ubiquitylation machinery. Ub attachment to substrates occurs through the sequential action of three classes of enzymes, E1s, E2s, and E3s. In humans, there are 2 E1s, ∼ 35 E2s, and hundreds of E3s that work to attach Ub to thousands of cellular substrates. Regulation of ubiquitylation can occur at each stage of the stepwise Ub transfer process, and substrates can also impact their own modification. Recent studies have revealed elegant mechanisms that have evolved to control the activity of the enzymes involved. In this minireview, we highlight recent discoveries that define some of the various mechanisms by which the activities of E3-Ub ligases are regulated.

Indexed as

AnimalsCullin ProteinsHumansModels, MolecularUbiquitinUbiquitinationUbiquitin-Protein LigasesCullin Proteinsparkin proteinUbiquitinUbiquitin-Protein LigasescullinE3 ubiquitin ligaseHECTparkinRINGubiquitinubiquitin ligaseubiquitin regulationubiquitylation (ubiquitination)

Identifiers

PMID26187467
PMCPMC4571856

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.