title: Extensive shape shifting underlies functional versatility of arrestins.
abstract: 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.
authors.affiliation: Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA. Electronic address: vsevolod.gurevich@vanderbilt.edu.
authors.forename: Vsevolod V
authors.initials: VV
authors.lastname: Gurevich
authors.affiliation: Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
authors.forename: Eugenia V
authors.initials: EV
authors.lastname: Gurevich
mesh_terms: D000818:Animals; D019390:Arrestins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D019390:Arrestins; D043562:Receptors, G-Protein-Coupled