About this Research Topic
Since its first application more than a decade ago, BRET has become a method of choice to monitor protein-protein interactions in live cells. In the seven transmembrane receptors (7TMRs) and receptor tyrosine kinases (RTK) field, it has been widely used to monitor i) receptor homo- /hetero-dimerization, ii) ligand-induced conformational changes in receptors, and iii) activation-promoted receptor complex formation with intracellular protein partners or structural rearrangements within the preassembled receptor signaling complexes. BRET technology has also been successfully utilized in the development of technological platforms for compound medium/high-throughput screening and biosensor technology.
We welcome submissions (reviews, research articles, methods, perspectives, etc.) that address the most recent advances in BRET technology and its utilization in the following areas of receptor-protein interactions investigation:
- Receptor homo- and hetero-oligomerization (specificity of BRET results, functional importance, negative cooperativity, allosteric modulation, dimer asymmetry ...)
- Conformational rearrangements within the receptor (e.g. movement of the third intracellular loop) and/or in the preassembled multiprotein signaling complexes
- Ligand-biased signaling (intramolecular BRET)
- Receptor screening challenges (BRET-based screening platforms for the TMRs and RTK)
- Biosensor development (tissue-based biosensors and their use in living subjects)
Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.