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

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A high-throughput nanoimmunoassay chip applied to large-scale vaccine adjuvant screening

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

CD44-specific supramolecular hydrogels for fluorescence molecular imaging of stem-like gastric cancer cells

Microdevice array-based identification of distinct mechanobiological response profiles in layer-specific valve interstitial cells

Rapid and automated multidimensional fluorescence microscopy profiling of 3D human breast cultures

Sorting single satellite cells from individual myofibers reveals heterogeneity in cell-surface markers and myogenic capacity

Human triple cell co-culture for evaluation of bone implant materials

Live cell imaging in a micro-array of acoustic traps facilitates quantification of natural killer cell heterogeneity

High-content adhesion assay to address limited cell samples

Stress response of Caenorhabditis elegans induced by space crowding in a micro-column array chip

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

Content Provider	Royal Society of Chemistry (RSC)
Author	Retterer, S. Stabley, D. Marshall, S. Salaita, K.
Copyright Year	2013
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 μm2) of ligand–receptor complex generated lower EGF receptor phosphorylation per ligand than smaller assemblies (<1 μm2) 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.
Starting Page	659
Ending Page	668
Page Count	10
File Format	HTM / HTML PDF
ISSN	17579694
Volume Number	5
Issue Number	4
Journal	Integrative Biology
DOI	10.1039/c3ib20239a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	EGF EGFR Growth factor Cell surface receptor Epidermal growth factor receptor Ligand Phosphorylation Lipid Diffusion Cytoskeleton Endocytosis Gefitinib
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Biophysics

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Manipulating the Lateral Diffusion of Surface-Anchored EGF Demonstrates that Receptor Clustering Modulates Phosphorylation Levels

Ligand-activated epidermal growth factor receptor (EGFR) signaling governs endocytic trafficking of unliganded receptor monomers by non-canonical phosphorylation

Transforming growth factor fi modulates phosphorylation of the epidermal growth factor receptor and proliferation of a431 cells’.

Mekada E: Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling

Allosteric regulation of epidermal growth factor (EGF) receptor ligand binding by tyrosine kinase inhibitors

The EGFR demonstrates linear signal transmission

Exploring higher-order EGFR oligomerisation and phosphorylation—a combined experimental and theoretical approach

Allosteric regulation of epidermal growth factor (EGF) receptor ligand binding by tyrosine kinase inhibitors

Nanoconjugation: a materials approach to enhance epidermal growth factor induced apoptosis

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

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Manipulating the Lateral Diffusion of Surface-Anchored EGF Demonstrates that Receptor Clustering Modulates Phosphorylation Levels

Ligand-activated epidermal growth factor receptor (EGFR) signaling governs endocytic trafficking of unliganded receptor monomers by non-canonical phosphorylation

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