New roles for beta-arrestins in cell signaling: not just for seven-transmembrane receptors.

Published

Journal Article (Review)

beta-arrestins, originally discovered as molecules that bind to and desensitize the activated and phosphorylated form of the G protein-coupled beta2-adrenergic receptor (beta2-AR), have recently emerged as multifunctional adaptor/scaffold proteins that dynamically assemble a wide range of multiprotein complexes in response to stimulation of most seven-transmembrane receptors (7TMRs). These complexes mediate receptor signaling, trafficking, and degradation. Moreover, beta-arrestins are increasingly found to perform analogous functions for receptors from structurally diverse classes, including atypical 7TMRs such as frizzled and smoothened, the nicotinic cholinergic receptors, receptor tyrosine kinases, and cytokine receptors, thereby regulating a growing list of cellular processes such as chemotaxis, apoptosis, and metastasis.

Full Text

Duke Authors

Cited Authors

  • Lefkowitz, RJ; Rajagopal, K; Whalen, EJ

Published Date

  • December 8, 2006

Published In

Volume / Issue

  • 24 / 5

Start / End Page

  • 643 - 652

PubMed ID

  • 17157248

Pubmed Central ID

  • 17157248

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2006.11.007

Language

  • eng

Conference Location

  • United States