Transactivation of G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs): Recent insights using luminescence and fluorescence technologies

Kilpatrick, Laura E.; Hill, Stephen J.

Abstract

© 2020 The Authors Alterations in signalling due to bidirectional transactivation of G protein-coupled receptor (GPCRs) and receptor tyrosine kinases (RTKs) are well established. Transactivation significantly diversifies signalling networks within a cell and has been implicated in promoting both advantageous and disadvantageous physiological and pathophysiological outcomes, making the GPCR/RTK interactions attractive new targets for drug discovery programmes. Transactivation has been observed for a plethora of receptor pairings in multiple cell types; however, the precise molecular mechanisms and signalling effectors involved can vary with receptor pairings and cell type. This short review will discuss the recent applications of proximity-based assays, such as resonance energy transfer and fluorescence-based imaging in investigating the dynamics of GPCR/RTK complex formation, subsequent effector protein recruitment and the cellular locations of complexes in living cells.

Citation

Kilpatrick, L. E., & Hill, S. J. (2021). Transactivation of G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs): Recent insights using luminescence and fluorescence technologies. Current Opinion in Endocrine and Metabolic Research, 16, 102-112. https://doi.org/10.1016/j.coemr.2020.10.003

• Journal Article Type: Article
• Acceptance Date: Oct 12, 2020
• Online Publication Date: Oct 22, 2020
• Publication Date: Feb 1, 2021
• Deposit Date: Oct 28, 2020
• Publicly Available Date: Oct 28, 2020
• Journal: Current Opinion in Endocrine and Metabolic Research
• Print ISSN: 2451-9650
• Electronic ISSN: 2451-9650
• Publisher: Elsevier
• Peer Reviewed: Peer Reviewed
• Volume: 16
• Pages: 102-112
• DOI: https://doi.org/10.1016/j.coemr.2020.10.003
• Keywords: G protein-coupled receptor; Receptor tyrosine kinase; Transactivation; Resonance energy transfer; Endocytosis; Oligomeric complexes
• Public URL: https://nottingham-repository.worktribe.com/output/4986481
• Publisher URL: https://www.sciencedirect.com/science/article/pii/S2451965020301046?via%3Dihub