Cargando…
β-Arrestin–Dependent Endocytosis of Proteinase-Activated Receptor 2 Is Required for Intracellular Targeting of Activated Erk1/2
Recently, a requirement for β-arrestin–mediated endocytosis in the activation of extracellular signal–regulated kinases 1 and 2 (ERK1/2) by several G protein–coupled receptors (GPCRs) has been proposed. However, the importance of this requirement for function of ERK1/2 is unknown. We report that ago...
Autores principales: | DeFea, K.A., Zalevsky, J., Thoma, M.S., Déry, O., Mullins, R.D., Bunnett, N.W. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2000
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174299/ https://www.ncbi.nlm.nih.gov/pubmed/10725339 |
Ejemplares similares
-
Beta-arrestin inhibits CAMKKbeta-dependent AMPK activation downstream of protease-activated-receptor-2
por: Wang, Ping, et al.
Publicado: (2010) -
Core engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation
por: Kumari, Punita, et al.
Publicado: (2017) -
C781, a β-Arrestin Biased Antagonist at Protease-Activated Receptor-2 (PAR2), Displays in vivo Efficacy Against Protease-Induced Pain in Mice
por: Kume, Moeno, et al.
Publicado: (2023) -
Smoothened determines β-arrestin–mediated removal of the G protein–coupled receptor Gpr161 from the primary cilium
por: Pal, Kasturi, et al.
Publicado: (2016) -
Phosphorylation of β-arrestin2 at Thr(383) by MEK underlies β-arrestin-dependent activation of Erk1/2 by GPCRs
por: Cassier, Elisabeth, et al.
Publicado: (2017)