Evidence map›Paper›PMID 33577797›Full record

ArticleThe Journal of biological chemistry

The ubiquitin isopeptidase USP10 deubiquitinates LC3B to increase LC3B levels and autophagic activity.

Rui Jia, Juan S Bonifacino

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
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  7. Identification of Key Active Constituents inInternational journal of molecular sciences · 2025
    Article
  8. Article
  9. Ethyl acetate extract ofFrontiers in pharmacology · 2025
    Article
  10. Article
  11. Article
  12. Ubiquitination in the regulation of autophagy.Acta biochimica et biophysica Sinica · 2023
    Article
  13. Article
  14. USP10 Alleviates Palmitic Acid-induced Steatosis through Autophagy in HepG2 Cells.Journal of clinical and translational hepatology · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Article
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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

2 authors at 1 institution in 1 country.

Rui JiaNeurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, USA. Electronic address: rui.jia@nih.gov.
Juan S BonifacinoNeurosciences and Cellular and Structural Biology Division, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, USA.
National Institutes of Health · US

Funding

Protein Trafficking In The Endosomal-Lysosomal SystemZIAHD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2025
$48.3M
Intramural NIH HHS ZIA HD001607
6 · The paper itself

Abstract

Components of the autophagy machinery are subject to regulation by various posttranslational modifications. Previous studies showed that monoubiquitination of LC3B catalyzed by the ubiquitin-activating enzyme UBA6 and ubiquitin-conjugating enzyme/ubiquitin ligase BIRC6 targets LC3B for proteasomal degradation, thus reducing LC3B levels and autophagic activity under conditions of stress. However, mechanisms capable of counteracting this process are not known. Herein, we report that LC3B ubiquitination is reversed by the action of the deubiquitinating enzyme USP10. We identified USP10 in a CRISPR-Cas9 knockout screen for ubiquitination-related genes that regulate LC3B levels. Biochemical analyses showed that silencing of USP10 reduces the levels of both the LC3B-I and LC3B-II forms of LC3B through increased ubiquitination and proteasomal degradation. In turn, the reduced LC3B levels result in slower degradation of the autophagy receptors SQSTM1 and NBR1 and an increased accumulation of puromycin-induced aggresome-like structures. Taken together, these findings indicate that the levels of LC3B and autophagic activity are controlled through cycles of LC3B ubiquitination and deubiquitination.

Indexed as

AutophagyCell LineCell Line, TumorEndopeptidasesHumansInhibitor of Apoptosis ProteinsIntracellular Signaling Peptides and ProteinsMicrotubule-Associated ProteinsProtein Processing, Post-TranslationalSequestosome-1 ProteinUbiquitin-Activating EnzymesUbiquitinationUbiquitin ThiolesteraseBIRC6 protein, humanEndopeptidasesInhibitor of Apoptosis ProteinsIntracellular Signaling Peptides and ProteinsMAP1LC3B protein, humanMicrotubule-Associated ProteinsNBR1 protein, humanSequestosome-1 ProteinSQSTM1 protein, humanUbiquitin-Activating Enzymesubiquitin isopeptidaseUbiquitin ThiolesteraseUSP10 protein, humanautophagyCRISPR/casdeubiquitinationLC3protein aggregationubiquitinUSP10

Identifiers

PMID33577797
PMCPMC7960534
OpenAlexW3127587726

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.