Arrestin-centred interactions at the membrane and their conformational determinants.

Autor: Underwood O; Division of Physiology, Pharmacology and Neuroscience, School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, UK.; Centre of Membrane Protein and Receptors, Universities of Birmingham and Nottingham, Midlands, UK., Haider RS; Division of Physiology, Pharmacology and Neuroscience, School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, UK.; Centre of Membrane Protein and Receptors, Universities of Birmingham and Nottingham, Midlands, UK., Sanchez J; Division of Physiology, Pharmacology and Neuroscience, School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, UK.; Centre of Membrane Protein and Receptors, Universities of Birmingham and Nottingham, Midlands, UK., Canals M; Division of Physiology, Pharmacology and Neuroscience, School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, UK.; Centre of Membrane Protein and Receptors, Universities of Birmingham and Nottingham, Midlands, UK.
Jazyk: angličtina
Zdroj: British journal of pharmacology [Br J Pharmacol] 2024 Mar 13. Date of Electronic Publication: 2024 Mar 13.
DOI: 10.1111/bph.16331
Abstrakt: More than 30 years after their discovery, arrestins are recognised multiprotein scaffolds that play essential roles in G protein-coupled receptor (GPCR) regulation and signalling. Originally named for their capacity to hinder GPCR coupling to G proteins and facilitate receptor desensitisation, arrestins have emerged as key hubs for a myriad of other functions, including receptor internalisation and scaffolding of signalling complexes. Recent structural studies have started to provide snapshots of the complexes formed by GPCRs and arrestins, supporting a wealth of biochemical data delineating the molecular determinants of such interactions. Furthermore, biophysical techniques have also provided key information with regards to the basal and active conformations of arrestins, and how these are affected upon GPCR activation. Here, we review the most recent advances on our understanding of GPCR-arrestin complexes, from structure to interactions of arrestins with the lipid bilayer and other proteins. We also present an updated view on the development of tools to study the conformational flexibility of arrestins, with the potential to provide experimental data to describe the dynamic models of arrestin activation.
(© 2024 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of British Pharmacological Society.)
Databáze: MEDLINE
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