ArticleNature communications2015
Ligand regulation of a constitutively dimeric EGF receptor.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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Who cites it
25 citing papers in PubMed.
- Ligand regulation and function of preformed EGFR dimers.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Computational design of synthetic receptors with programmable signalling activity for enhanced cancer T cell therapy.Nature biomedical engineering · 2026Article
- EGFR: New Insights on Its Activation and Mutation in Tumor and Tumor Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- The Physiological and Pathological Mechanisms of LIN2, LIN7, LIN10 and Their Tripartite Complex.Journal of cellular and molecular medicine · 2025Review
- A critical evaluation of protein kinase regulation by activation loop autophosphorylation.eLife · 2023Article
- A perspective of fluorescence microscopy for cellular structural biology with EGFR as witness.Journal of microscopy · 2023Article
- EGFR signal transduction is downregulated in C. elegans vulval precursor cells during dauer diapause.Development (Cambridge, England) · 2022Article
- LAG3 ectodomain structure reveals functional interfaces for ligand and antibody recognition.Nature immunology · 2022Article
- CD99-PTPN12 Axis Suppresses Actin Cytoskeleton-Mediated Dimerization of Epidermal Growth Factor Receptor.Cancers · 2020Article
- Insulin and epidermal growth factor receptor family members share parallel activation mechanisms.Protein science : a publication of the Protein Society · 2020Review
- Emerging Allosteric Mechanism of EGFR Activation in Physiological and Pathological Contexts.Biophysical journal · 2019Review
- Complex Formation between VEGFR2 and the βCell chemical biology · 2019Article
- Oncogenic mutations at the EGFR ectodomain structurally converge to remove a steric hindrance on a kinase-coupled cryptic epitope.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Review
- A Brief History of Single-Particle Tracking of the Epidermal Growth Factor Receptor.Methods and protocols · 2019Review
- The architecture of EGFR's basal complexes reveals autoinhibition mechanisms in dimers and oligomers.Nature communications · 2018Article
- Visualization of ligand-induced transmembrane signaling in the full-length human insulin receptor.The Journal of cell biology · 2018Article
- Regulation of Kinase Activity in the Caenorhabditis elegans EGF Receptor, LET-23.Structure (London, England : 1993) · 2018Article
- Piecing it together: Unraveling the elusive structure-function relationship in single-pass membrane receptors.Biochimica et biophysica acta. Biomembranes · 2017Review
- Dynamic Modulation of Binding Affinity as a Mechanism for Regulating Interferon Signaling.Journal of molecular biology · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Ligand-induced receptor dimerization has traditionally been viewed as the key event in transmembrane signalling by epidermal growth factor receptors (EGFRs). Here we show that the Caenorhabditis elegans EGFR orthologue LET-23 is constitutively dimeric, yet responds to its ligand LIN-3 without changing oligomerization state. SAXS and mutational analyses further reveal that the preformed dimer of the LET-23 extracellular region is mediated by its domain II dimerization arm and resembles other EGFR extracellular dimers seen in structural studies. Binding of LIN-3 induces only minor structural rearrangements in the LET-23 dimer to promote signalling. Our results therefore argue that EGFR can be regulated by allosteric changes within an existing receptor dimer--resembling signalling by insulin receptor family members, which share similar extracellular domain compositions but form covalent dimers.
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Registered trials
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.