Evidence map›Paper›PMID 32265230›Full record

ReviewJournal of cell science2020

HECT E3 ubiquitin ligases - emerging insights into their biological roles and disease relevance.

Yaya Wang, Diana Argiles-Castillo, Emma I Kane, Anning Zhou, Donald E Spratt

Erratum issuedOpen access · bronzeAbstract readReview
In one paragraph

Review in Journal of cell science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

88 citing papers in PubMed, 128 citations in OpenAlex.

  1. E3 Ubiquitin Ligases in MASH-Associated Liver Fibrosis: Mechanisms and Therapeutic Opportunities.Liver international : official journal of the International Association for the Study of the Liver · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Unraveling the impact ofBrain communications · 2026
    Article
  8. Review
  9. Article
  10. Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity.International journal of molecular sciences · 2025
    Review
  11. SMURF2 inhibits autophagic control ofbioRxiv : the preprint server for biology · 2025
    Article
  12. The E3 ligase HECTD4 regulates COX-2-dependent tumor progression and metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Emerging roles for E3 ubiquitin ligases in neural development and disease.Frontiers in cell and developmental biology · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

28 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Yaya WangCollege of Chemistry and Chemical Engineering, Xi'an University of Science and Technology, Xi'an, Shanxi, China 710054.
Diana Argiles-CastilloGustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St., Worcester, MA 01610, USA.
Emma I KaneGustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St., Worcester, MA 01610, USA.
Anning ZhouCollege of Chemistry and Chemical Engineering, Xi'an University of Science and Technology, Xi'an, Shanxi, China 710054.
Donald E SprattGustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St., Worcester, MA 01610, USA dspratt@clarku.edu.ORCID 0000-0002-0699-155X
Clark University · USXi'an University of Science and Technology · CN

Funding

Structure and Mechanism of HERC5-dependent ISGylationR15GM126432 · NIGMS · CLARK UNIVERSITY (WORCESTER, MA) · PI SPRATT, DONALD ERIC · 2017 to 2023
$1000k
NIGMS NIH HHS R15 GM126432
6 · The paper itself

Abstract

Homologous to E6AP C-terminus (HECT) E3 ubiquitin ligases play a critical role in various cellular pathways, including but not limited to protein trafficking, subcellular localization, innate immune response, viral infections, DNA damage responses and apoptosis. To date, 28 HECT E3 ubiquitin ligases have been identified in humans, and recent studies have begun to reveal how these enzymes control various cellular pathways by catalyzing the post-translational attachment of ubiquitin to their respective substrates. New studies have identified substrates and/or interactors with different members of the HECT E3 ubiquitin ligase family, particularly for E6AP and members of the neuronal precursor cell-expressed developmentally downregulated 4 (NEDD4) family. However, there still remains many unanswered questions about the specific roles that each of the HECT E3 ubiquitin ligases have in maintaining cellular homeostasis. The present Review discusses our current understanding on the biological roles of the HECT E3 ubiquitin ligases in the cell and how they contribute to disease development. Expanded investigations on the molecular basis for how and why the HECT E3 ubiquitin ligases recognize and regulate their intracellular substrates will help to clarify the biochemical mechanisms employed by these important enzymes in ubiquitin biology.

Indexed as

UbiquitinUbiquitin-Protein LigasesHumansProtein Processing, Post-TranslationalUbiquitinationUbiquitinUbiquitin-Protein LigasesCancerCell signalingE3 ubiquitin ligaseHECTNeurodegenerationNeurodevelopmental disordersNeurological disordersProtein-protein interactionsProtein turnoverUbiquitinUbiquitylation

Identifiers

PMID32265230
PMCPMC7157599
OpenAlexW3014889276

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.