ArticleBiochimica et biophysica acta. General subjects2017
Cooperative interactions between VEGFR2 extracellular Ig-like subdomains ensure VEGFR2 dimerization.
Article in Biochimica et biophysica acta. General subjects, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- VEGFR2 dimerization kinetics on the cell surface determined by microscopy and mathematical modeling.Biophysical journal · 2026Article
- Vascular endothelial growth factor signaling in health and disease: from molecular mechanisms to therapeutic perspectives.Signal transduction and targeted therapy · 2025Review
- OPN3-mediated positive regulation of angiogenesis in HUVECs through VEGFR2 interaction.Communications biology · 2025Article
- Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane.The Biochemical journal · 2021Article
- Neural network strategies for plasma membrane selection in fluorescence microscopy images.Biophysical journal · 2021Article
- The Biased Ligands NGF and NT-3 Differentially Stabilize Trk-A Dimers.Biophysical journal · 2021Article
- Revisiting a controversy: The effect of EGF on EGFR dimer stability.Biochimica et biophysica acta. Biomembranes · 2020Article
- Direct measurements of VEGF-VEGFR2 binding affinities reveal the coupling between ligand binding and receptor dimerization.The Journal of biological chemistry · 2019Article
- Dimerization of the Trk receptors in the plasma membrane: effects of their cognate ligands.The Biochemical journal · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundPrior studies have suggested that the interactions occurring between VEGFR2 extracellular domains in the absence of ligand are complex. Here we seek novel insights into these interactions, and into the role of the different Ig-like domains (D1 through D7) in VEGFR2 dimerization.
methodsWe study the dimerization of a single amino acid mutant and of three deletion mutants in the plasma membrane using two photon microscopy and fully quantified spectral imaging.
resultsWe demonstrate that a set of cooperative interactions between the different Ig-like domains ensure that VEGFR2 dimerizes with a specific affinity instead of forming oligomers.
conclusionsThe contributions of subunits D7 and D4 seem to be the most critical, as they appear essential for strong lateral interactions and for the formation of dimers, respectively. GENERAL SIGNIFICANCE: This study provides new insights into the mechanism of VEGFR2 dimerization and activation.
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