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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.

SUBMITTER: Gurevich VV

PROVIDER: S-EPMC3971385 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Extensive shape shifting underlies functional versatility of arrestins.

Gurevich Vsevolod V VV Gurevich Eugenia V EV

Current opinion in cell biology 20131116

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 vari ...[more]

PMID: 24680424

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