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Independent β-Arrestin 2 and G Protein-Mediated Pathways for Angiotensin II Activation of Extracellular Signal-Regulated Kinases 1 and 2
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Independent β-Arrestin 2 and G Protein-Mediated Pathways for Angiotensin II Activation of Extracellular Signal-Regulated Kinases 1 and 2
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Independent β-Arrestin 2 and G Protein-Mediated Pathways for Angiotensin II Activation of Extracellular Signal-Regulated Kinases 1 and 2
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Journal Article
Independent β-Arrestin 2 and G Protein-Mediated Pathways for Angiotensin II Activation of Extracellular Signal-Regulated Kinases 1 and 2
2003
Overview
Stimulation of a mutant angiotensin type 1A receptor (DRY/AAY) with angiotensin II (Ang II) or of a wild-type receptor with an Ang II analog ([sarcosine1,Ile4,Ile8]Ang II) fails to activate classical heterotrimeric G protein signaling but does lead to recruitment of β-arrestin 2-GFP and activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) (maximum stimulation ≈50% of wild type). This G protein-independent activation of mitogen-activated protein kinase is abolished by depletion of cellular β-arrestin 2 but is unaffected by the PKC inhibitor Ro-31-8425. In parallel, stimulation of the wild-type angiotensin type 1A receptor with Ang II robustly stimulates ERK1/2 activation with ≈60% of the response blocked by the PKC inhibitor (G protein dependent) and the rest of the response blocked by depletion of cellular β-arrestin 2 by small interfering RNA (β-arrestin dependent). These findings imply the existence of independent G protein- and β-arrestin 2-mediated pathways leading to ERK1/2 activation and the existence of distinct \"active\" conformations of a seven-membrane-spanning receptor coupled to each.
Publisher
National Academy of Sciences,National Acad Sciences
