ArticleMolecular and cellular biology2011
Human epidermal growth factor receptor (EGFR) aligned on the plasma membrane adopts key features of Drosophila EGFR asymmetry.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- Drug-resistant EGFR mutations promote lung cancer by stabilizing interfaces in ligand-free kinase-active EGFR oligomers.Nature communications · 2024Article
- A perspective of fluorescence microscopy for cellular structural biology with EGFR as witness.Journal of microscopy · 2023Article
- Fluorescence Imaging of Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor Resistance in Non-Small Cell Lung Cancer.Cancers · 2022Review
- The architecture of EGFR's basal complexes reveals autoinhibition mechanisms in dimers and oligomers.Nature communications · 2018Article
- EGFR oligomerization organizes kinase-active dimers into competent signalling platforms.Nature communications · 2016Article
- The Dipole Potential Modifies the Clustering and Ligand Binding Affinity of ErbB Proteins and Their Signaling Efficiency.Scientific reports · 2016Article
- pH dependence of ligand-induced human epidermal growth factor receptor activation investigated by molecular dynamics simulations.Journal of molecular modeling · 2016Article
- Enhanced dimerization drives ligand-independent activity of mutant epidermal growth factor receptor in lung cancer.Molecular biology of the cell · 2015Article
- Compounds identified by virtual docking to a tetrameric EGFR extracellular domain can modulate Grb2 internalization.BMC cancer · 2015Article
- A structural perspective on the regulation of the epidermal growth factor receptor.Annual review of biochemistry · 2015Review
- Putting together structures of epidermal growth factor receptors.Current opinion in structural biology · 2014Review
- Membrane interaction of bound ligands contributes to the negative binding cooperativity of the EGF receptor.PLoS computational biology · 2014Article
- Recruitment of the adaptor protein Grb2 to EGFR tetramers.Biochemistry · 2014Article
- Physiological epidermal growth factor concentrations activate high affinity receptors to elicit calcium oscillations.PloS one · 2014Article
- Ligand binding and dynamics of the monomeric epidermal growth factor receptor ectodomain.Proteins · 2013Article
- Dynamic transition states of ErbB1 phosphorylation predicted by spatial stochastic modeling.Biophysical journal · 2013Article
- Article
- A single ligand is sufficient to activate EGFR dimers.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Finding the missing links in EGFR.Nature structural & molecular biology · 2012Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
The ability of epidermal growth factor receptor (EGFR) to control cell fate is defined by its affinity for ligand. Current models suggest that ligand-binding heterogeneity arises from negative cooperativity in signaling receptor dimers, for which the asymmetry of the extracellular region of the Drosophila EGFR has recently provided a structural basis. However, no asymmetry is apparent in the isolated extracellular region of the human EGFR. Human EGFR also differs from the Drosophila EGFR in that negative cooperativity is found only in full-length receptors in cells. To gain structural insights into the human EGFR in situ, we developed an approach based on quantitative Förster resonance energy transfer (FRET) imaging, combined with Monte Carlo and molecular dynamics simulations, to probe receptor conformation in epithelial cells. We experimentally demonstrate a high-affinity ligand-binding human EGFR conformation consistent with the extracellular region aligned flat on the plasma membrane. We explored the relevance of this conformation to ligand-binding heterogeneity and found that the asymmetry of this structure shares key features with that of the Drosophila EGFR, suggesting that the structural basis for negative cooperativity is conserved from invertebrates to humans but that in human EGFR the extracellular region asymmetry requires interactions with the plasma membrane.
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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.