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Annual Review of Physiology

Volume 69, 2007

β-Arrestins and Cell Signaling

Abstract

Abstract

Upon their discovery, β-arrestins 1 and 2 were named for their capacity to sterically hinder the G protein coupling of agonist-activated seven-transmembrane receptors, ultimately resulting in receptor desensitization. Surprisingly, recent evidence shows that β-arrestins can also function to activate signaling cascades independently of G protein activation. By serving as multiprotein scaffolds, the β-arrestins bring elements of specific signaling pathways into close proximity. β-Arrestin regulation has been demonstrated for an ever-increasing number of signaling molecules, including the mitogen-activated protein kinases ERK, JNK, and p38 as well as Akt, PI3 kinase, and RhoA. In addition, investigators are discovering new roles for β-arrestins in nuclear functions. Here, we review the signaling capacities of these versatile adapter molecules and discuss the possible implications for cellular processes such as chemotaxis and apoptosis.

Keyword(s): ERK, G protein–coupled receptor kinase, MAPK, phosphorylation, scaffold, seven-transmembrane receptor
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/content/journals/10.1146/annurev.physiol.69.022405.154749
2007-03-17
2024-04-25
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β-Arrestins and Cell Signaling
Annual Review of Physiology 69, 483 (2007); https://doi.org/10.1146/annurev.physiol.69.022405.154749
/content/journals/10.1146/annurev.physiol.69.022405.154749
/content/journals/10.1146/annurev.physiol.69.022405.154749
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  • Article Type: Review Article

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