Evidence map›Paper›PMID 32997988›Full record

ArticleCell reports2020

Heterogeneity in VEGF Receptor-2 Mobility and Organization on the Endothelial Cell Surface Leads to Diverse Models of Activation by VEGF.

Bruno da Rocha-Azevedo, Sungsoo Lee, Aparajita Dasgupta, Anthony R Vega, Luciana R de Oliveira, Tae Kim, Mark Kittisopikul, Zachariah A Malik, Khuloud Jaqaman

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

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  7. Single-Molecule FRET-Tracking of InlB-Activated MET Receptors in Living Cells.Small (Weinheim an der Bergstrasse, Germany) · 2026
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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

9 authors at 3 institutions in 1 country.

Bruno da Rocha-AzevedoDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Sungsoo LeeDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Aparajita DasguptaDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Anthony R VegaDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA; Lyda Hill Department of Bioinformatics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Luciana R de OliveiraDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Tae KimDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Mark KittisopikulDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Zachariah A MalikDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Khuloud JaqamanDepartment of Biophysics, UT Southwestern Medical Center, Dallas, TX 75390, USA; Lyda Hill Department of Bioinformatics, UT Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: khuloud.jaqaman@utsouthwestern.edu.
Southwestern Medical CenterSouthwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

Mechanisms and Functional Consequences of Signaling Protein Organization at MembranesR35GM119619 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI DASGUPTA, APARAJITA KAMALESH · 2016 to 2025
$4.3M
NIGMS NIH HHS R35 GM119619
6 · The paper itself

Abstract

The dynamic nanoscale organization of cell surface receptors plays an important role in signaling. We determine this organization and its relation to activation of VEGF receptor-2 (VEGFR-2), a critical receptor tyrosine kinase in endothelial cells (ECs), by combining single-molecule imaging of endogenous VEGFR-2 in live ECs with multiscale computational analysis. We find that surface VEGFR-2 can be mobile or exhibit restricted mobility and be monomeric or non-monomeric, with a complex interplay between the two. This basal heterogeneity results in heterogeneity in the sequence of steps leading to VEGFR-2 activation by VEGF. Specifically, we find that VEGF can bind to monomeric and non-monomeric VEGFR-2 and that, when binding to monomeric VEGFR-2, its effect on dimerization depends on the mobility of VEGFR-2. Our study highlights the dynamic and heterogeneous nature of cell surface receptor organization and the need for multiscale, single-molecule-based analysis to determine its relationship to receptor activation and signaling.

Indexed as

Cell ProliferationEndothelial CellsHumansSignal TransductionVascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth Factor Receptor-2angiogenesiscomputational analysismulti-scalenanoscaleparticle trackingquantitative microscopysingle-molecule imagingspatiotemporalstochasticVEGFR

Identifiers

PMID32997988
PMCPMC7541195
OpenAlexW3089416259

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.