Differential β-arrestin binding of AT1 and AT2 angiotensin receptors

40Citations
Citations of this article
36Readers
Mendeley users who have this article in their library.

Abstract

Agonist stimulation of G protein-coupled receptors causes receptor activation, phosphorylation, β-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 β-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. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Cite

CITATION STYLE

APA

Turu, G., Szidonya, L., Gáborik, Z., Buday, L., Spät, A., Clark, A. J. L., & Hunyady, L. (2006). Differential β-arrestin binding of AT1 and AT2 angiotensin receptors. FEBS Letters, 580(1), 41–45. https://doi.org/10.1016/j.febslet.2005.11.044

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free