ArticleScience (New York, N.Y.)2023
Time-resolved live-cell spectroscopy reveals EphA2 multimeric assembly.
Article in Science (New York, N.Y.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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Who cites it
31 citing papers in PubMed, 43 citations in OpenAlex.
- Structural organization of TAM receptor ectodomains.The Biochemical journal · 2026Article
- Structural basis of phosphatidylserine enhancement of Gas6 ligand-induced Axl activation.bioRxiv : the preprint server for biology · 2026Article
- Pseudorabies virus pUL40 drives inflammatory signaling through competitive hijacking of EphA2 from the Akt-EphA2 interaction.Veterinary research · 2026Article
- Mechanisms and Manifestations of Ligand Bias in Signaling: Focus on Receptor Tyrosine Kinases.Chemical reviews · 2026Review
- SUMOylation of EphB4 enhances its stability in prostate cancer.British journal of cancer · 2026Article
- EPHA2-Ephrin-B1 cis-interaction drives an oncogenic reverse signaling, leading to the recurrence of oral cancer.Cell communication and signaling : CCS · 2026Article
- An MIEN1-based hexamer peptide (LA3IK) inhibits EGF-driven oncogenic signaling in prostate cancer by disrupting EGFR-ERBB2 heterodimerization.Scientific reports · 2026Article
- Prosaposin orchestrates a TGFβ1-driven paracrine loop between Schwann cells and gastric cancer to accelerate perineural invasion.Journal of experimental & clinical cancer research : CR · 2026Article
- Fluorescence Correlation Spectroscopy to Examine Protein-Lipid Interactions in Membranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Frequent EPHA2 receptor mutations in cholangiocarcinoma disrupt receptor forward signaling supporting a tumor suppressor role.Biochimica et biophysica acta. Molecular cell research · 2026Article
- FRET-FCS: Advancing comprehensive insights into complex biological systems.Biophysical journal · 2025Review
- Exogenous ephrin-A3 reverses loss of vaginal epithelial barrier protection in progestin-treated mice.Mucosal immunology · 2025Article
- Progress and Prospects in FRET for the Investigation of Protein-Protein Interactions.Biosensors · 2025Review
- Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025Review
- EphA2 and Ephrin-A1 Utilize the Same Interface for BothbioRxiv : the preprint server for biology · 2025Article
- Cholesterol-dependent dimerization and conformational dynamics of EphA2 receptors from coarse-grained and all-atom simulations.Structure (London, England : 1993) · 2025Article
- NMR resonance assignment of a ligand-binding domain of ephrin receptor A2.Biomolecular NMR assignments · 2025Article
- Synthetic antibodies targeting EphA2 induce diverse signaling-competent clusters with differential activation.Protein science : a publication of the Protein Society · 2025Article
- Article
- Recent Advances in Augmenting the Therapeutic Efficacy of Peptide-Drug Conjugates.Journal of medicinal chemistry · 2025Review
Corrections and comments
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Authors and funding
16 authors at 8 institutions in 1 country.
Funding
Abstract
Ephrin type-A receptor 2 (EphA2) is a receptor tyrosine kinase that initiates both ligand-dependent tumor-suppressive and ligand-independent oncogenic signaling. We used time-resolved, live-cell fluorescence spectroscopy to show that the ligand-free EphA2 assembles into multimers driven by two types of intermolecular interactions in the ectodomain. The first type entails extended symmetric interactions required for ligand-induced receptor clustering and tumor-suppressive signaling that inhibits activity of the oncogenic extracellular signal-regulated kinase (ERK) and protein kinase B (AKT) protein kinases and suppresses cell migration. The second type is an asymmetric interaction between the amino terminus and the membrane proximal domain of the neighboring receptors, which supports oncogenic signaling and promotes migration in vitro and tumor invasiveness in vivo. Our results identify the molecular interactions that drive the formation of the EphA2 multimeric signaling clusters and reveal the pivotal role of EphA2 assembly in dictating its opposing functions in oncogenesis.
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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.