FRET

An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.

Publication

Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy.

McVey M, Ramsay D, Kellett E, Rees S, Wilson S, Pope AJ, Milligan G

Oligomerization of the human delta-opioid receptor and its regulation by ligand occupancy were explored following expression in HEK293 cells using each of co-immunoprecipitation of differentially epitope-tagged forms of the receptor, bioluminescence resonance energy transfer and time-resolved fluorescence resonance energy transfer. All of the approaches identified constitutively formed receptor oligomers, and the time-resolved fluorescence studies confirmed the presence of such homo-oligomers ... [more]

J. Biol. Chem. Apr. 27, 2001; 276(17);14092-9 [Pubmed: 11278447]

Throughput

  • Low Throughput

Additional Notes

  • Protein interactions were detected using bioluminescence resonance energy transfer (BRET).

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ADRB2 ADRB2
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Low-BioGRID
3206311

Curated By

  • BioGRID