Extensive shape shifting underlies functional versatility of arrestins.

Gurevich VV, Gurevich EV
Curr Opin Cell Biol. 2014 27: 1-9

PMID: 24680424 · PMCID: PMC3971385 · DOI:10.1016/j.ceb.2013.10.007

Among four vertebrate arrestins, only two are ubiquitously expressed. Arrestins specifically bind active phosphorylated G protein-coupled receptors (GPCRs), thereby precluding further G protein activation. Recent discoveries suggest that the formation of the arrestin-receptor complex initiates the second round of signaling with comparable biological importance. Despite having virtually no recognizable sequence motifs known to mediate protein-protein interactions, arrestins bind a surprising variety of signaling proteins with mind-boggling range of functional consequences. High conformational flexibility allows arrestins to show many distinct 'faces' to the world, which allows these relatively small ∼45kDa proteins to bind various partners under different physiological conditions, organizing multi-protein signaling complexes and localizing them to distinct subcellular compartments.

Copyright © 2013 Elsevier Ltd. All rights reserved.

MeSH Terms (8)

Animals Arrestins Humans Phosphorylation Protein Binding Protein Conformation Receptors, G-Protein-Coupled Signal Transduction

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