Evidence map›Paper›PMID 26459808›Full record

ArticleTraffic (Copenhagen, Denmark)2016

VEGFR2 Trafficking, Signaling and Proteolysis is Regulated by the Ubiquitin Isopeptidase USP8.

Gina A Smith, Gareth W Fearnley, Izma Abdul-Zani, Stephen B Wheatcroft, Darren C Tomlinson, Michael A Harrison, Sreenivasan Ponnambalam

Open access · hybridAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. KIF13B mediates VEGFR2 recycling to modulate vascular permeability.Cellular and molecular life sciences : CMLS · 2023
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Lipid Raft Association Stabilizes VEGF Receptor 2 in Endothelial Cells.International journal of molecular sciences · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2.International journal of molecular sciences · 2018
    Review
  18. Review
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Gina A SmithEndothelial Cell Biology Unit, School of Molecular & Cellular Biology, University of Leeds, LS2 9JT, Leeds, UK.
Gareth W FearnleyEndothelial Cell Biology Unit, School of Molecular & Cellular Biology, University of Leeds, LS2 9JT, Leeds, UK.
Izma Abdul-ZaniEndothelial Cell Biology Unit, School of Molecular & Cellular Biology, University of Leeds, LS2 9JT, Leeds, UK.
Stephen B WheatcroftLeeds Institute of Cardiovascular & Metabolic Medicine, University of Leeds, LS2 9JT, Leeds, UK.
Darren C TomlinsonBiomedical Health Research Centre & Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, Leeds, UK.
Michael A HarrisonSchool of Biomedical Sciences, University of Leeds, LS2 9JT, Leeds, UK.
Sreenivasan PonnambalamEndothelial Cell Biology Unit, School of Molecular & Cellular Biology, University of Leeds, LS2 9JT, Leeds, UK.
University of Leeds · GBInstitute of Structural and Molecular Biology · GB

Funding

British Heart Foundation FS/12/20/29462Medical Research Council
6 · The paper itself

Abstract

Vascular endothelial growth factor A (VEGF-A) regulates many aspects of vascular function. VEGF-A binding to vascular endothelial growth factor receptor 2 (VEGFR2) stimulates endothelial signal transduction and regulates multiple cellular responses. Activated VEGFR2 undergoes ubiquitination but the enzymes that regulate this post-translational modification are unclear. In this study, the de-ubiquitinating enzyme, USP8, is shown to regulate VEGFR2 trafficking, de-ubiquitination, proteolysis and signal transduction. USP8-depleted endothelial cells displayed altered VEGFR2 ubiquitination and production of a unique VEGFR2 extracellular domain proteolytic fragment caused by VEGFR2 accumulation in the endosome-lysosome system. In addition, perturbed VEGFR2 trafficking impaired VEGF-A-stimulated signal transduction in USP8-depleted cells. Thus, regulation of VEGFR2 ubiquitination and de-ubiquitination has important consequences for the endothelial cell response and vascular physiology.

Indexed as

ProteolysisSignal TransductionEndopeptidasesEndosomal Sorting Complexes Required for TransportEndosomesHumansHuman Umbilical Vein Endothelial CellsProtein TransportUbiquitinationUbiquitin ThiolesteraseVascular Endothelial Growth Factor Receptor-2EndopeptidasesEndosomal Sorting Complexes Required for TransportKDR protein, humanUbiquitin ThiolesteraseUSP8 protein, humanVascular Endothelial Growth Factor Receptor-2de-ubiquitinationproteolysissignal transductiontraffickingUSP8VEGF-AVEGFR2

Identifiers

PMID26459808
PMCPMC4832373
OpenAlexW2175236682

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.