Beta-arrestins and Cell Signaling

Annu Rev Physiol. 2007;69:483-510. doi: 10.1146/annurev.physiol.69.022405.154749.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Arrestins / physiology*
  • Arrestins / ultrastructure
  • Biotransformation / physiology
  • Cell Nucleus / physiology
  • Extracellular Signal-Regulated MAP Kinases / physiology
  • Humans
  • Janus Kinases / physiology
  • Mitogen-Activated Protein Kinases / physiology
  • Phosphorylation
  • Protein Conformation
  • Signal Transduction / physiology*
  • beta-Arrestins
  • p38 Mitogen-Activated Protein Kinases / physiology

Substances

  • Arrestins
  • beta-Arrestins
  • Janus Kinases
  • Extracellular Signal-Regulated MAP Kinases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases