ArticleBiochemical and biophysical research communications2015
Lateral diffusion contributes to FRET from lanthanide-tagged membrane proteins.
Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Acceleration of antibacterial activity of curcumin loaded biopolymers against methicillin-resistantEngineering in life sciences · 2022Article
- Differential Aggregation Properties of Mutant Human and Bovine Rhodopsin.Biochemistry · 2021Article
- Lanthanide-Based Optical Probes of Biological Systems.Cell chemical biology · 2020Review
- Agonist-induced membrane nanodomain clustering drives GLP-1 receptor responses in pancreatic beta cells.PLoS biology · 2019Article
- Detection of misfolded rhodopsin aggregates in cells by Förster resonance energy transfer.Methods in cell biology · 2019Article
- Misfolded rhodopsin mutants display variable aggregation properties.Biochimica et biophysica acta. Molecular basis of disease · 2018Article
- Wild-type opsin does not aggregate with a misfolded opsin mutant.Biochimica et biophysica acta · 2016Article
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Authors and funding
3 authors.
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Abstract
Diffusion can enhance Förster resonance energy transfer (FRET) when donors or acceptors diffuse distances that are similar to the distances separating them during the donor's excited state lifetime. Lanthanide donors remain in the excited state for milliseconds, which makes them useful for time-resolved FRET applications but also allows time for diffusion to enhance energy transfer. Here we show that diffusion dramatically enhances FRET between membrane proteins labeled with lanthanide donors. This phenomenon complicates interpretation of experiments that use long-lived donors to infer association or proximity of mobile membrane proteins, but also offers a method of monitoring diffusion in membrane domains in real time in living cells.
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