Role of β-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking

Curr Opin Cell Biol. 2014 Apr;27:63-71. doi: 10.1016/j.ceb.2013.11.005. Epub 2013 Dec 14.

Abstract

The arrestin clan can now be broadly divided into three structurally similar subgroups: the originally identified arrestins (visual and β-arrestins), the α-arrestins and a group of Vps26-related proteins. The visual and β-arrestins selectively bind to agonist-occupied phosphorylated G protein-coupled receptors (GPCRs) and inhibit GPCR coupling to heterotrimeric G proteins while the β-arrestins also function as adaptor proteins to regulate GPCR trafficking and G protein-independent signaling. The α-arrestins have also recently been implicated in regulating GPCR trafficking while Vps26 regulates retrograde trafficking. In this review, we provide an overview of the α-arrestins and β-arrestins with a focus on our current understanding of how these adaptor proteins regulate GPCR trafficking.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Arrestins / chemistry*
  • Arrestins / metabolism*
  • Endocytosis
  • Humans
  • Models, Molecular
  • Phosphorylation
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Protein Transport
  • Receptors, G-Protein-Coupled / metabolism*
  • Signal Transduction
  • beta-Arrestins

Substances

  • Arrestins
  • Receptors, G-Protein-Coupled
  • beta-Arrestins