ArticleBiophysical journal2006
Determination of the two-dimensional interaction rate constants of a cytokine receptor complex.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 56 citations in OpenAlex.
- Mechanisms of enhanced or impaired DNA target selectivity driven by protein dimerization.PNAS nexus · 2026Article
- Assembly of Macromolecular Complexes in the Whole-Cell Model of a Minimal Cell.The journal of physical chemistry. B · 2026Article
- A membrane-driven biochemical oscillator tunable by the volume to surface area ratio.bioRxiv : the preprint server for biology · 2025Article
- Protein dimerization in 2D vs 3D: Geometric allostery enhances binding affinity.The Journal of chemical physics · 2025Article
- Mechanisms of enhanced or impaired DNA target selectivity driven by protein dimerization.bioRxiv : the preprint server for biology · 2025Article
- Kinetic study of membrane protein interactions: from three to two dimensions.Scientific reports · 2024Article
- Dual-color DNA-PAINT single-particle tracking enables extended studies of membrane protein interactions.Nature communications · 2023Article
- Optimal ligand discrimination by asymmetric dimerization and turnover of interferon receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins.eLife · 2021Article
- Quantitative systems pharmacology of interferon alpha administration: A multi-scale approach.PloS one · 2019Article
- Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments.Nature communications · 2017Article
- Receptor dimer stabilization by hierarchical plasma membrane microcompartments regulates cytokine signaling.Science advances · 2016Article
- Article
- Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling.The Journal of cell biology · 2015Article
- Structure of the Toll-Spatzle complex, a molecular hub in Drosophila development and innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Ligand-independent interaction of the type I interferon receptor complex is necessary to observe its biological activity.Cytokine · 2013Article
- Structural basis of a unique interferon-β signaling axis mediated via the receptor IFNAR1.Nature immunology · 2013Article
- Microcantilever-Based Label-Free Characterization of Temperature-Dependent Biomolecular Affinity Binding.Sensors and actuators. B, Chemical · 2013Article
- Redirecting cell-type specific cytokine responses with engineered interleukin-4 superkines.Nature chemical biology · 2012Article
- Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation.Immunological reviews · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ligand-receptor interactions within the plane of the plasma membrane play a pivotal role for transmembrane signaling. The biophysical principles of protein-protein interactions on lipid bilayers, though, have hardly been experimentally addressed. We have dissected the interactions involved in ternary complex formation by ligand-induced cross-linking of the subunits of the type I interferon (IFN) receptors ifnar1 and ifnar2 in vitro. The extracellular domains ifnar1-ectodomain (EC) and ifnar2-EC were tethered in an oriented manner on solid-supported lipid bilayers. The interactions of IFNalpha2 and several mutants, which exhibit different association and dissociation rate constants toward ifnar1-EC and ifnar2-EC, were monitored by simultaneous label-free detection and surface-sensitive fluorescence spectroscopy. Surface dissociation rate constants were determined by measuring ligand exchange kinetics, and by measuring receptor exchange on the surface by fluorescence resonance energy transfer. Strikingly, approximately three-times lower dissociation rate constants were observed for both receptor subunits compared to the dissociation in solution. Based on these directly determined surface-dissociation rate constants, the surface-association rate constants were assessed by probing ligand dissociation at different relative surface concentrations of the receptor subunits. In contrast to the interaction in solution, the association rate constants depended on the orientation of the receptor components. Furthermore, the large differences in association kinetics observed in solution were not detectable on the surface. Based on these results, the key roles of orientation and lateral diffusion on the kinetics of protein interactions in plane of the membrane are discussed.
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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.