Differential beta-arrestin binding of AT1 and AT2 angiotensin receptors

FEBS Lett. 2006 Jan 9;580(1):41-5. doi: 10.1016/j.febslet.2005.11.044. Epub 2005 Dec 6.

Abstract

Agonist stimulation of G protein-coupled receptors causes receptor activation, phosphorylation, beta-arrestin binding and receptor internalization. Angiotensin II (AngII) causes rapid internalization of the AT1 receptors, whereas AngII-bound AT2 receptors do not internalize. Although the activation of the rat AT1A receptor with AngII causes translocation of beta-arrestin2 to the receptor, no association of this molecule with the AT2 receptor can be detected after AngII treatment with confocal microscopy or bioluminescence resonance energy transfer. These data demonstrate that the two subtypes of angiotensin receptors have different mechanisms of regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin II / metabolism
  • Angiotensin II / pharmacology*
  • Animals
  • Arrestins / metabolism*
  • Cell Line
  • Humans
  • Microscopy, Confocal
  • Phosphorylation / drug effects
  • Protein Binding / drug effects
  • Protein Binding / physiology
  • Protein Transport / drug effects
  • Protein Transport / physiology
  • Rats
  • Receptor, Angiotensin, Type 1 / agonists*
  • Receptor, Angiotensin, Type 1 / metabolism
  • Receptor, Angiotensin, Type 2 / agonists*
  • Receptor, Angiotensin, Type 2 / metabolism
  • Signal Transduction / drug effects
  • Signal Transduction / physiology
  • Vasoconstrictor Agents / metabolism
  • Vasoconstrictor Agents / pharmacology*
  • beta-Arrestins

Substances

  • Arrestins
  • Receptor, Angiotensin, Type 1
  • Receptor, Angiotensin, Type 2
  • Vasoconstrictor Agents
  • beta-Arrestins
  • Angiotensin II