Journal
CURRENT OPINION IN CELL BIOLOGY
Volume 27, Issue -, Pages 63-71Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.ceb.2013.11.005
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Funding
- National Institutes of Health [GM44944, GM47417, HL114471]
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The arrestin clan can now be broadly divided into three structurally similar subgroups: the originally identified arrestins (visual and beta-arrestins), the alpha-arrestins and a group of Vps26-related proteins. The visual and beta-arrestins selectively bind to agonist-occupied phosphorylated G protein-coupled receptors (GPCRs) and inhibit GPCR coupling to heterotrimeric G proteins while the beta-arrestins also function as adaptor proteins to regulate GPCR trafficking and G protein-independent signaling. The alpha-arrestins have also recently been implicated in regulating GPCR trafficking while Vps26 regulates retrograde trafficking. In this review, we provide an overview of the alpha-arrestins and beta-arrestins with a focus on our current understanding of how these adaptor proteins regulate GPCR trafficking.
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