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

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-couple...

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Bibliographic Details
Published in:Current opinion in cell biology 2014-04, Vol.27, p.63-71
Main Authors: Kang, Dong Soo, Tian, Xufan, Benovic, Jeffrey L
Format: Article
Language:English
Subjects:
Animals
Arrestins - chemistry
Arrestins - metabolism
beta-Arrestins
Endocytosis
Humans
Internal Medicine
Models, Molecular
Phosphorylation
Protein Binding
Protein Processing, Post-Translational
Protein Structure, Tertiary
Protein Transport
Receptors, G-Protein-Coupled - metabolism
Signal Transduction
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Summary: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.
ISSN:0955-0674
1879-0410
DOI:10.1016/j.ceb.2013.11.005