Format

Send to

Choose Destination
Curr Opin Cell Biol. 2014 Apr;27:1-9. doi: 10.1016/j.ceb.2013.10.007. Epub 2013 Nov 16.

Extensive shape shifting underlies functional versatility of arrestins.

Author information

1
Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA. Electronic address: vsevolod.gurevich@vanderbilt.edu.
2
Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.

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.

PMID:
24680424
PMCID:
PMC3971385
DOI:
10.1016/j.ceb.2013.10.007
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center