ArticleiScience2025
Ligand preference of EphB2 receptor is selectively regulated by N-glycosylation.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Morphometric profiling and EphB2/B4 and ephrin-B1 membrane protein expression analysis in vesicular, bulbourethral, and preputial glands in mice.Journal of advanced veterinary and animal research · 2026Article
- Discovery of Sennoside A as a NaturalResearch (Washington, D.C.) · 2026Article
- TM9SF4 acts as a receptor mediatingFrontiers in cellular and infection microbiology · 2026Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Eph receptors and their ephrin ligands play important roles in cell communication and neuron development. Eph interacts with ephrin in a complex manner. Here, we found ephrin-B2 instead of well-recorded ephrin-A5 specifically recognize and activate EphB2 receptor in primary cortical neurons. Domain-swapping and N/Q mutagenesis results show that the ectodomain of EphB2 and its N-glycosylation sites are critical for the ephrin binding selectivity. The N265, N336, N428, and N482Q mutant EphB2 cannot distinguish ephrin-B2 from ephrin-A5. Furthermore, the N-glycosylation sites in EphB2 are evolutionarily conserved and the N-glycan-directed binding strategy is commonly used in other Eph family members. A gain-of-function EphB6 mutant restores its ephrin-B2 binding ability. Finally, EphB2 is robustly glycosylated in the mouse brain and N-glycosylation is required for EphB2 signaling-induced cell rounding and dendritic spine formation. Collectively, our findings provide a molecular basis to understand the exquisite Eph/ephrin interaction preferences.
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