Evidence map›Paper›PMID 23416883›Full record

ArticleIntegrative biology : quantitative biosciences from nano to macro2013

Manipulating the lateral diffusion of surface-anchored EGF demonstrates that receptor clustering modulates phosphorylation levels.

D Stabley, S Retterer, S Marshall, K Salaita

Open access · greenAbstract read
In one paragraph

Article in Integrative biology : quantitative biosciences from nano to macro, 2013. 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
4.0field-weighted citation impact, top 7% 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, 36 citations in OpenAlex.

  1. Clustering of Membrane Receptors: Insights from DNA Origami-Based Approaches.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Review
  2. Article
  3. Manipulation of PD-L1 Endosomal Trafficking Promotes Anticancer Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  4. Article
  5. Review
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  10. Topography design in model membranes: Where biology meets physics.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
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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 2 institutions in 1 country.

D StableyDepartment of Chemistry, Emory University, Atlanta, GA, USA.
S Retterer
S Marshall
K Salaita
Emory University · USOak Ridge National Laboratory · US

Funding

Elucidating the Biophysical Mechanisms of Notch ActivationR01GM097399 · NIGMS · EMORY UNIVERSITY · PI SALAITA, KHALID S. · 2012 to 2016
$1.6M
NHLBI NIH HHS HHSN268201000043CNIGMS NIH HHS R01 GM097399NIGMS NIH HHS R01-GM097399-01
6 · The paper itself

Abstract

Upon activation, the epidermal growth factor (EGF) receptor becomes phosphorylated and triggers a vast signaling network that has profound effects on cell growth. The EGF receptor is observed to assemble into clusters after ligand binding and tyrosine kinase autophosphorylation, but the role of these assemblies in the receptor signaling pathway remains unclear. To address this question, we measured the phosphorylation of EGFR when the EGF ligand was anchored onto laterally mobile and immobile surfaces. We found that cells generated clusters of ligand-receptor complex on mobile EGF surfaces, and displayed a lower ratio of phosphorylated EGFR to EGF when compared to immobilized EGF that is unable to cluster. This result was verified by tuning the lateral assembly of ligand-receptor complexes on the surface of living cells using patterned supported lipid bilayers. Nanoscale metal lines fabricated into the supported membrane constrained lipid diffusion and EGF receptor assembly into micron and sub-micron scale corrals. Single cell analysis indicated that clustering impacts EGF receptor activation, and larger clusters (>1 μm(2)) of ligand-receptor complex generated lower EGF receptor phosphorylation per ligand than smaller assemblies (<1 μm(2)) in HCC1143 cells that were engaged to ligand-functionalized surfaces. We investigated the mechanism of EGFR clustering by treating cells with compounds that disrupt the cytoskeleton (Latrunculin B), clathrin-mediated endocytosis (Pitstop2), and inhibit EGFR activation (Gefitinib). These results help elucidate the nature of large-scale EGFR clustering, thus underscoring the general significance of receptor spatial organization in tuning biochemical function.

Indexed as

Biocompatible MaterialsBreast NeoplasmsDiffusionEpidermal Growth FactorErbB ReceptorsFemaleHumansPhosphorylationProtein BindingSignal TransductionSurface PropertiesTumor Cells, CulturedUp-RegulationBiocompatible MaterialsEpidermal Growth FactorErbB Receptors

Identifiers

PMID23416883
PMCPMC3609930
OpenAlexW2153231341

What OpenQuestion holds

Textmetadata
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.