ArticleNature structural & molecular biology2011
Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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88 citing papers in PubMed, 149 citations in OpenAlex.
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- Active regulation of the epidermal growth factor receptor by the membrane bilayer.bioRxiv : the preprint server for biology · 2025Article
- Structural analysis of HER2-trastuzumab complex reveals receptor conformational adaptation.Science advances · 2025Article
- Drug-resistant EGFR mutations promote lung cancer by stabilizing interfaces in ligand-free kinase-active EGFR oligomers.Nature communications · 2024Article
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- Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure and dynamics of the EGFR/HER2 heterodimer.Cell discovery · 2023Article
- Structural arrangement of the active back-to-back dimer in N-glycosylated ErbB receptors is regulated by heterodimerization.Molecular biology research communications · 2023Article
- Inactivating Amplified HER2: Challenges, Dilemmas, and Future Directions.Cancer research · 2022Article
- Ligand-induced transmembrane conformational coupling in monomeric EGFR.Nature communications · 2022Article
- Ligands with different dimeric configurations potently activate the EphA2 receptor and reveal its potential for biased signaling.iScience · 2022Article
- Protection of the Prodomain α1-Helix Correlates with Latency in the Transforming Growth Factor-β Family.Journal of molecular biology · 2022Article
- A Dual-Color Fluorescent Probe Allows Simultaneous Imaging of Main and Papain-like Proteases of SARS-CoV-2-Infected Cells for Accurate Detection and Rapid Inhibitor Screening.Angewandte Chemie (International ed. in English) · 2022Article
- Extensive conformational and physical plasticity protects HER2-HER3 tumorigenic signaling.Cell reports · 2022Article
- An effective strategy for ligand-mediated pulldown of the HER2/HER3/NRG1β heterocomplex and cryo-EM structure determination at low sample concentrations.Methods in enzymology · 2022Article
- Efficient expression, purification, and visualization by cryo-EM of unliganded near full-length HER3.Methods in enzymology · 2022Article
- Allosteric activation of preformed EGF receptor dimers by a single ligand binding event.Frontiers in endocrinology · 2022Article
- Pondering the mechanism of receptor tyrosine kinase activation: The case for ligand-specific dimer microstate ensembles.Current opinion in structural biology · 2021Review
28 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
To our knowledge, no structural study to date has characterized, in an intact receptor, the coupling of conformational change in extracellular domains through a single-pass transmembrane domain to conformational change in cytoplasmic domains. Here we examine such coupling, and its unexpected complexity, using nearly full-length epidermal growth factor receptor (EGFR) and negative-stain EM. The liganded, dimeric EGFR ectodomain can couple both to putatively active, asymmetrically associated kinase dimers and to putatively inactive, symmetrically associated kinase dimers and monomers. Inhibitors that stabilize the active or inactive conformation of the kinase active site, as well as mutations in the kinase dimer interface and a juxtamembrane phosphorylation site, shift the equilibrium among the three kinase association states. This coupling of one conformation of an activated receptor ectodomain to multiple kinase-domain arrangements reveals previously unanticipated complexity in transmembrane signaling and facilitates regulation of receptor function in the juxtamembrane and cytoplasmic environments.
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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.