Evidence map›Paper›PMID 21539813›Full record

ArticleBiochemical and biophysical research communications2011

The VEGFR2 receptor tyrosine kinase undergoes constitutive endosome-to-plasma membrane recycling.

Helen M Jopling, Gareth J Howell, Nikita Gamper, Sreenivasan Ponnambalam

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  7. Purification and Analysis of Circulating Lipid Particles.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Article
  9. Lipid Raft Association Stabilizes VEGF Receptor 2 in Endothelial Cells.International journal of molecular sciences · 2021
    Article
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  14. Article
  15. Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2.International journal of molecular sciences · 2018
    Review
  16. 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

4 authors at 1 institution in 1 country.

Helen M JoplingEndothelial Cell Biology Unit, Institute of Molecular and Cellular Biology, University of Leeds, LIGHT Laboratories, Clarendon Way, Leeds LS2 9JT, UK.
Gareth J Howell
Nikita Gamper
Sreenivasan Ponnambalam
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research CouncilBritish Heart FoundationWellcome Trust
6 · The paper itself

Abstract

The VEGFR2 receptor tyrosine kinase regulates vascular physiology and animal development. The mechanism underlying VEGFR2 membrane trafficking is not well understood. Herein, we show that VEGFR2 undergoes membrane recycling in both vascular and non-vascular cells. In primary human endothelial cells, VEGFR2 normally distributes between the plasma membrane and early endosomes undergoing endocytosis and recycling. This pathway is independent of VEGFR tyrosine kinase activity and occurs constitutively, similar to other integral membrane proteins such as the transferrin receptor and β1 integrin. Expression of a VEGFR2-EGFP hybrid protein in non-vascular cells revealed plasma membrane and endosome distribution. The VEGF-A ligand stimulated phosphorylation of residue Y1175 on VEGFR2-EGFP which is a key hallmark of receptor activation. Live cell imaging and quantitative analysis showed that activated VEGFR2-EGFP displayed reduced mobility linked to endocytosis and recycling between the plasma membrane and endosomes. Total internal reflection microscopy and kinetics indicates that VEGFR2 undergoes recycling between the plasma membrane and peripheral endosomes proximal to the membrane bilayer. We thus provide evidence that the VEGFR2 receptor tyrosine kinase undertakes a constitutive recycling pathway between the peripheral endosomes and cell surface and this exists in both vascular and non-vascular cells.

Indexed as

Cell MembraneCells, CulturedEndocytosisEndosomesEndothelial CellsEndothelium, VascularHEK293 CellsHumansVascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth Factor Receptor-2

Identifiers

PMID21539813
PMCPMC6103438
OpenAlexW2141801986

What OpenQuestion holds

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LicenceTDM
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.