Independent β-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2
Semmelweis University · Cleveland Clinic · +3 more institutions
Abstract
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 beta-arrestin 2-GFP and activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) (maximum stimulation approximately 50% of wild type). This G protein-independent activation of mitogen-activated protein kinase is abolished by depletion of cellular beta-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…
Citation impact
- FWCI
- 8.13
- Percentile
- 100%
- References
- 30
Authors
7- HWHuijun WeiCorresponding
Semmelweis University, Cleveland Clinic, Howard Hughes Medical Institute, Duke Medical Center, Duke University Hospital
- SASeungkirl Ahn
Semmelweis University, Cleveland Clinic, Howard Hughes Medical Institute, Duke Medical Center, Duke University Hospital
- SKSudha K. Shenoy
Semmelweis University, Cleveland Clinic, Howard Hughes Medical Institute, Duke Medical Center, Duke University Hospital
- SSSadashiva S. Karnik
Semmelweis University, Cleveland Clinic, Howard Hughes Medical Institute, Duke Medical Center, Duke University Hospital
- LHLászló Hunyady
Semmelweis University, Cleveland Clinic, Howard Hughes Medical Institute, Duke Medical Center, Duke University Hospital
Topics & keywords
- Heterotrimeric G protein
- Angiotensin II
- Cell biology
- G protein-coupled receptor kinase
- Gq alpha subunit
- Arrestin
- Kinase
- Signal transduction