Beta-arrestins and cell signaling.

Journal Article (Review)

Upon their discovery, beta-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 beta-arrestins can also function to activate signaling cascades independently of G protein activation. By serving as multiprotein scaffolds, the beta-arrestins bring elements of specific signaling pathways into close proximity. beta-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 beta-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.

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

PubMed ID

  • 17305471

International Standard Serial Number (ISSN)

  • 0066-4278

Digital Object Identifier (DOI)

  • 10.1146/annurev.ph.69.013107.100021

Language

  • eng

Conference Location

  • United States