Arrestin interaction with E3 ubiquitin ligases and deubiquitinases: functional and therapeutic implications.

Journal Article (Journal Article)

Arrestins constitute a small family of four homologous adaptor proteins (arrestins 1-4), which were originally identified as inhibitors of signal transduction elicited by the seven-transmembrane G protein-coupled receptors. Currently arrestins (especially arrestin2 and arrestin3; also called β-arrestin1 and β-arrestin2) are known to be activators of cell signaling and modulators of endocytic trafficking. Arrestins mediate these effects by binding to not only diverse cell-surface receptors but also by associating with a variety of critical signaling molecules in different intracellular compartments. Thus, the functions of arrestins are multifaceted and demand interactions with a host of proteins and require an array of selective conformations. Furthermore, receptor ligands that specifically induce signaling via arrestins are being discovered and their physiological roles are emerging. Recent evidence suggests that the activity of arrestin is regulated in space and time by virtue of its dynamic association with specific enzymes of the ubiquitination pathway. Ubiquitin-dependent, arrestin-mediated signaling could serve as a potential platform for developing novel therapeutic strategies to target transmembrane signaling and physiological responses.

Full Text

Duke Authors

Cited Authors

  • Shenoy, SK

Published Date

  • 2014

Published In

Volume / Issue

  • 219 /

Start / End Page

  • 187 - 203

PubMed ID

  • 24292831

International Standard Serial Number (ISSN)

  • 0171-2004

Digital Object Identifier (DOI)

  • 10.1007/978-3-642-41199-1_10


  • eng

Conference Location

  • Germany