ArticleThe Journal of biological chemistry2013
Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Synthetic antibodies targeting EphA2 induce diverse signaling-competent clusters with differential activation.Protein science : a publication of the Protein Society · 2025Article
- Review
- The Ephb2 Receptor Uses Homotypic, Head-to-Tail Interactions within Its Ectodomain as an Autoinhibitory Control Mechanism.International journal of molecular sciences · 2021Article
- Article
- Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors.International journal of molecular sciences · 2021Review
- In-depth Site-specific Analysis of N-glycoproteome in Human Cerebrospinal Fluid and Glycosylation Landscape Changes in Alzheimer's Disease.Molecular & cellular proteomics : MCP · 2021Article
- A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.Molecular syndromology · 2020Article
- Tumor Necrosis Factor Alpha-Induced Proteins in Malignant Tumors: Progress and Prospects.OncoTargets and therapy · 2020Review
- EphA2 contributes to disruption of the blood-brain barrier in cerebral malaria.PLoS pathogens · 2020Article
- Identification of Targets to Redirect CAR T Cells in Glioblastoma and Colorectal Cancer: An Arduous Venture.Frontiers in immunology · 2020Review
- Glycosylation Changes in Brain Cancer.ACS chemical neuroscience · 2018Review
- Asymmetry at cell-cell interfaces direct cell sorting, boundary formation, and tissue morphogenesis.Experimental cell research · 2017Review
- Glycoengineering of EphA4 Fc leads to a unique, long-acting and broad spectrum, Eph receptor therapeutic antagonist.Scientific reports · 2017Article
- Enhancing Irreversible Electroporation by Manipulating Cellular Biophysics with a Molecular Adjuvant.Biophysical journal · 2017Article
- EphA2 is a functional receptor for the growth factor progranulin.The Journal of cell biology · 2016Article
- Simultaneous targeting of Eph receptors in glioblastoma.Oncotarget · 2016Article
- Integrated Transcriptomic and Glycomic Profiling of Glioma Stem Cell Xenografts.Journal of proteome research · 2015Article
- Ephs and Ephrins in malignant gliomas.Growth factors (Chur, Switzerland) · 2014Review
- Eph- and ephrin-dependent mechanisms in tumor and stem cell dynamics.Cellular and molecular life sciences : CMLS · 2014Review
- Multireceptor targeting of glioblastoma.Neuro-oncology advancesArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The EphA2 receptor tyrosine kinase is overexpressed in a number of malignancies and is activated by ephrin ligands, most commonly by ephrin-A1. The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1. Here we report for the first time the significance of the glycosylation in the biology of EphA2 and ephrin-A1. Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2. We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation. Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity. Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization. Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136. These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
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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.