ArticleProceedings of the National Academy of Sciences of the United States of America2013
Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 73 citations in OpenAlex.
- Structural organization of TAM receptor ectodomains.The Biochemical journal · 2026Article
- Molecular Determinants of Receptor-Specific Membrane Interactions in EphA1 and EphA2 from Coarse-Grained Simulations.Journal of chemical information and modeling · 2026Article
- The multifaceted roles of receptor tyrosine pseudokinases in cellular signalling.Biochemical Society transactions · 2026Review
- Synthetic antibodies targeting EphA2 induce diverse signaling-competent clusters with differential activation.Protein science : a publication of the Protein Society · 2025Article
- AlphaPPIweb: an integration platform for protein-protein interaction prediction and evaluation.American journal of cancer research · 2025Article
- Constrained β-Hairpins Targeting the EphA4 Ligand Binding Domain.Journal of medicinal chemistry · 2024Article
- Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024Review
- Co-clustering of EphB6 and ephrinB1 in trans restrains cancer cell invasion.Communications biology · 2024Article
- Eph receptors and ephrins in cancer progression.Nature reviews. Cancer · 2024Review
- Time-resolved live-cell spectroscopy reveals EphA2 multimeric assembly.Science (New York, N.Y.) · 2023Article
- Ephrin-Eph receptor tyrosine kinases for potential therapeutics against hepatic pathologies.Journal of cell communication and signaling · 2023Review
- Structural insights into EphA4 unconventional activation from prediction of the EphA4 and its complex with ribonuclease 1.American journal of cancer research · 2022Article
- Molecular evolution and signatures of selective pressures on Bos, focusing on the Nelore breed (Bos indicus).PloS one · 2022Article
- The Ephb2 Receptor Uses Homotypic, Head-to-Tail Interactions within Its Ectodomain as an Autoinhibitory Control Mechanism.International journal of molecular sciences · 2021Article
- NMR-Guided Design of Potent and Selective EphA4 Agonistic Ligands.Journal of medicinal chemistry · 2021Article
- Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors.International journal of molecular sciences · 2021Review
- A cancer mutation promotes EphA4 oligomerization and signaling by altering the conformation of the SAM domain.The Journal of biological chemistry · 2021Article
- Effective Tumor Targeting by EphA2-Agonist-Biotin-Streptavidin Conjugates.Molecules (Basel, Switzerland) · 2021Article
- Molecular Inversion Probe-Based Sequencing ofInternational journal of molecular sciences · 2021Article
- Nogo-A-Δ20/EphA4 interaction antagonizes apoptosis of neural stem cells by integrating p38 and JNK MAPK signaling.Journal of molecular histology · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Eph receptor tyrosine kinases and their ephrin ligands mediate cell signaling during normal and oncogenic development. Eph signaling is initiated in a multistep process leading to the assembly of higher-order Eph/ephrin clusters that set off bidirectional signaling in interacting cells. Eph and ephrins are divided in two subclasses based on their abilities to bind and activate each other and on sequence conservation. EphA4 is an exception to the general rule because it can be activated by both A- and B-class ephrin ligands. Here we present high-resolution structures of the complete EphA4 ectodomain and its complexes with ephrin-A5. The structures reveal how ligand binding promotes conformational changes in the EphA4 ligand-binding domain allowing the formation of signaling clusters at the sites of cell-cell contact. In addition, the structural data, combined with structure-based mutagenesis, reveal a previously undescribed receptor-receptor interaction between the EphA4 ligand-binding and membrane-proximal fibronectin domains, which is functionally important for efficient receptor activation.
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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.