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Differential β‐arrestin binding of AT 1 and AT 2 angiotensin receptors
Author(s) -
Turu Gábor,
Szidonya László,
Gáborik Zsuzsanna,
Buday László,
Spät András,
Clark Adrian J.L.,
Hunyady László
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.044
Subject(s) - internalization , receptor , angiotensin ii , angiotensin ii receptor type 1 , arrestin , microbiology and biotechnology , enzyme linked receptor , chemistry , g protein coupled receptor , agonist , angiotensin receptor , g protein coupled receptor kinase , endocrinology , biophysics , medicine , biology , biochemistry
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 AT 1 receptors, whereas AngII‐bound AT 2 receptors do not internalize. Although the activation of the rat AT 1A receptor with AngII causes translocation of β‐arrestin2 to the receptor, no association of this molecule with the AT 2 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.