Profiling novel pharmacology of receptor complexes using Receptor-HIT
Autor: | Kevin D. G. Pfleger, Elizabeth K. M. Johnstone |
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Rok vydání: | 2021 |
Předmět: |
Energy transfer
G-protein-coupled receptors Heteromer receptors Endogeny Biochemistry Receptor tyrosine kinase Receptors G-Protein-Coupled Biochemical Techniques & Resources Humans Bioluminescence Receptor Review Articles G protein-coupled receptor chemistry.chemical_classification Molecular Interactions biology Pharmacology & Toxicology Biomolecule intracellular signaling Receptor Protein-Tyrosine Kinases Signaling Cell biology Energy Transfer chemistry biology.protein BRET |
Zdroj: | Biochemical Society Transactions |
ISSN: | 1470-8752 0300-5127 |
Popis: | Many receptors are able to undergo heteromerisation, leading to the formation of receptor complexes that may have pharmacological profiles distinct from those of the individual receptors. As a consequence of this, receptor heteromers can be classed as new drug targets, with the potential for achieving greater specificity and selectivity over targeting their constituent receptors. We have developed the Receptor-Heteromer Investigation Technology (Receptor-HIT), which enables the detection of receptor heteromers using a proximity-based reporter system such as bioluminescence resonance energy transfer (BRET). Receptor-HIT detects heteromers in live cells and in real time, by utilising ligand-induced signals that arise from altered interactions with specific biomolecules, such as ligands or proteins. Furthermore, monitoring the interaction between the receptors and the specific biomolecules generates functional information about the heteromer that can be pharmacologically quantified. This review will discuss various applications of Receptor-HIT, including its use with different classes of receptors (e.g. G protein-coupled receptors (GPCRs), receptor tyrosine kinases (RTKs) and others), its use to monitor receptor interactions both intracellularly and extracellularly, and also its use with genome-edited endogenous proteins. |
Databáze: | OpenAIRE |
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