β-Arrestins and cell signaling

Journal Article

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. Copyright © 2007 by Annual Reviews. All rights reserved.

Full Text

Duke Authors

Cited Authors

  • DeWire, SM; Ahn, S; Lefkowitz, RJ; Shenoy, SK

Published Date

  • 2007

Published In

Volume / Issue

  • 69 /

Start / End Page

  • 483 - 510

International Standard Serial Number (ISSN)

  • 0066-4278

Digital Object Identifier (DOI)

  • 10.1146/annurev.physiol.69.022405.154749