Emerging paradigms of β-arrestin-dependent seven transmembrane receptor signaling

Trends Biochem Sci. 2011 Sep;36(9):457-69. doi: 10.1016/j.tibs.2011.06.003. Epub 2011 Jul 20.


β-Arrestins, originally discovered to desensitize activated seven transmembrane receptors (7TMRs; also known as G-protein-coupled receptors, GPCRs), are now well established mediators of receptor endocytosis, ubiquitylation and G protein-independent signaling. Recent global analyses of β-arrestin interactions and β-arrestin-dependent phosphorylation events have uncovered several previously unanticipated roles of β-arrestins in a range of cellular signaling events. These findings strongly suggest that the functional roles of β-arrestins are much broader than currently understood. Biophysical studies aimed at understanding multiple active conformations of the 7TMRs and the β-arrestins have begun to unravel the mechanistic basis for the diverse functional capabilities of β-arrestins in cellular signaling.

Publication types

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

MeSH terms

  • Angiotensin II / analogs & derivatives
  • Angiotensin II / metabolism
  • Animals
  • Arrestins / metabolism*
  • Endocytosis
  • Extracellular Signal-Regulated MAP Kinases / metabolism
  • Humans
  • Membrane Proteins / metabolism
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Protein Conformation
  • Protein Transport
  • Receptors, G-Protein-Coupled / metabolism*
  • Signal Transduction*
  • Species Specificity
  • Ubiquitination
  • beta-Arrestins


  • Arrestins
  • Membrane Proteins
  • Phosphoproteins
  • Receptors, G-Protein-Coupled
  • angiotensin II, Sar(1)-Ile(4)-Ile(8)-
  • beta-Arrestins
  • seven-transmembrane G-protein-coupled receptor
  • Angiotensin II
  • Extracellular Signal-Regulated MAP Kinases