期刊
FRONTIERS IN ENDOCRINOLOGY
卷 5, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fendo.2014.00026
关键词
bioluminescence resonance energy transfer; BRET; fluorescence resonance energy transfer; FRET; GPCR; GPCR-HIT; heteromer; Receptor-HIT
资金
- Australian Research Council (ARC) [DP120101297, LP130100037]
- Dimerix Bioscience Pty Ltd.
- University of Nottingham
- Promega Corporation
- BMG Labtech Pty Ltd. [LP130100037]
- ARC [FT100100271]
- Medical Research Council [G0800006]
- MRC [G0800006] Funding Source: UKRI
Guanine nucleotide binding protein (G protein)-coupled receptors (GPCRs) function in complexes with a range of molecules and proteins including ligands, G proteins, arrestins, ubiquitin, and other receptors. Elements of these complexes may interact constitutively or dynamically, dependent upon factors such as ligand binding, phosphorylation, and dephosphorylation. They may also be allosterically modulated by other proteins in a manner that changes temporally and spatially within the cell. Elucidating how these complexes function has been greatly enhanced by biophysical technologies that are able to monitor proximity and/or binding, often in real time and in live cells. These include resonance energy transfer approaches such as bioluminescence resonance energy transfer (BRET) and fluorescence resonance energy transfer (FRET). Furthermore, the use of fluorescent ligands has enabled novel insights into allosteric interactions between GPCRs. Consequently, biophysical approaches are helping to unlock the amazing diversity and bias in G protein-coupled receptor signaling.
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