ArticleBiophysical journal2023
Utility of FRET in studies of membrane protein oligomerization: The concept of the effective dissociation constant.
Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- A co-overexpression strategy allows effective protein-protein binding affinities to be assessed as a function of concentration within live cells.bioRxiv : the preprint server for biology · 2026Article
- Advances in FRET methodologies for probing molecular interactions.Biophysical journal · 2025Article
- Multimer Detection System: A Universal Assay System for Differentiating Protein Oligomers from Monomers.International journal of molecular sciences · 2025Review
- Transmembrane helix interactions regulate oligomerization of the receptor tyrosine kinase EphA2.The Journal of biological chemistry · 2024Article
- Investigations of membrane protein interactions in cells using fluorescence microscopy.Current opinion in structural biology · 2024Review
- Implementation of FRET Spectrometry Using Temporally Resolved Fluorescence: A Feasibility Study.International journal of molecular sciences · 2024Article
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Authors and funding
4 authors.
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Abstract
The activity of many membrane receptors is controlled through their lateral association into dimers or higher-order oligomers. Although Förster resonance energy transfer (FRET) measurements have been used extensively to characterize the stability of receptor dimers, the utility of FRET in studies of larger oligomers has been limited. Here we introduce an effective equilibrium dissociation constant that can be extracted from FRET measurements for EphA2, a receptor tyrosine kinase (RTK) known to form active oligomers of heterogeneous distributions in response to its ligand ephrinA1-Fc. The newly introduced effective equilibrium dissociation constant has a well-defined physical meaning and biological significance. It denotes the receptor concentration for which half of the receptors are monomeric and inactive, and the other half are associated into oligomers and are active, irrespective of the exact oligomer size. This work introduces a new dimension to the utility of FRET in studies of membrane receptor association and signaling in the plasma membrane.
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