Evidence map›Paper›PMID 28851806›Full record

ArticleJournal of cell science2017

The deubiquitylase USP10 regulates integrin β1 and β5 and fibrotic wound healing.

Stephanie R Gillespie, Liana J Tedesco, Lingyan Wang, Audrey M Bernstein

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

25 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. USP40 protects podocytes by deubiquitylating integrin β1.Biochemical and biophysical research communications · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Histology and histopathology · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. USP10 Promotes Fibronectin Recycling, Secretion, and Organization.Investigative ophthalmology & visual science · 2021
    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

4 authors at 1 institution in 1 country.

Stephanie R GillespieIcahn School of Medicine at Mount Sinai, Departments of Ophthalmology and Pharmacology and Systems Therapeutics, New York, NY 10029, USA.
Liana J TedescoIcahn School of Medicine at Mount Sinai, Departments of Ophthalmology and Pharmacology and Systems Therapeutics, New York, NY 10029, USA.ORCID http://orcid.org/0000-0001-5927-4469
Lingyan WangIcahn School of Medicine at Mount Sinai, Departments of Ophthalmology and Pharmacology and Systems Therapeutics, New York, NY 10029, USA.ORCID http://orcid.org/0000-0001-9236-7229
Audrey M BernsteinIcahn School of Medicine at Mount Sinai, Departments of Ophthalmology and Pharmacology and Systems Therapeutics, New York, NY 10029, USA bernstea@upstate.edu.ORCID http://orcid.org/0000-0002-2537-2594
Icahn School of Medicine at Mount Sinai · US

Funding

Teaching biomedical and pharmacological trainees to produce FAIR data for AI & ML applicationsT32GM062754 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI SCHLESSINGER, AVNER · 2001 to 2023
$6.2M
THE UBIQUITIN PATHWAY IN CORNEAL SCARRINGR01EY024942 · NEI · UPSTATE MEDICAL UNIVERSITY · PI AUDREY M BERNSTEIN · 2015 to 2026
$3.1M
NEI NIH HHS R01 EY024942NIGMS NIH HHS T32 GM062754
6 · The paper itself

Abstract

Scarring and fibrotic disease result from the persistence of myofibroblasts characterized by high surface expression of αv integrins and subsequent activation of the transforming growth factor β (TGFβ) proteins; however, the mechanism controlling their surface abundance is unknown. Genetic screening revealed that human primary stromal corneal myofibroblasts overexpress a subset of deubiquitylating enzymes (DUBs), which remove ubiquitin from proteins, preventing degradation. Silencing of the DUB USP10 induces a buildup of ubiquitin on integrins β1 and β5 in cell lysates, whereas recombinant USP10 removes ubiquitin from these integrin subunits. Correspondingly, the loss and gain of USP10 decreases and increases, respectively, αv/β1/β5 protein levels, without altering gene expression. Consequently, endogenous TGFβ is activated and the fibrotic markers alpha-smooth muscle actin (α-SMA) and cellular fibronectin (FN-EDA) are induced. Blocking either TGFβ signaling or cell-surface αv integrins after USP10 overexpression prevents or reduces fibrotic marker expression. Finally, silencing of USP10 in an

Indexed as

UbiquitinationAnimalsCells, CulturedHEK293 CellsHumansIntegrin beta1Integrin beta ChainsProteolysisSignal TransductionSus scrofaTissue Culture TechniquesTransforming Growth Factor betaUbiquitin ThiolesteraseWound HealingIntegrin beta1Integrin beta ChainsITGB5 protein, humanTransforming Growth Factor betaUbiquitin ThiolesteraseUSP10 protein, humanFibrosisIntegrinMyofibroblastScarringWound healing

Identifiers

PMID28851806
PMCPMC5665446
OpenAlexW2750640253

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.