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- W76819147 abstract "Some G-protein coupled receptors (GPCRs) can activate extracellular signal regulated kinases 1 and 2 (ERK1/2) through the formation of β-arrestin scaffolds. Two such receptors, protease activated receptor-2 (PAR-2) and neurokinin 1 receptor (NK1R), promote β-arrestin-dependent ERK1/2 activation, but the scaffolding complexes formed differ in their composition, stability, and subcellular localization. While PAR-2 promotes cytosolic retention of activated ERK1/2 through association with β-arrestins leading to cell motility, NK1R promotes nuclear translocation of ERK1/2 and proliferation. To examine the possibility that the C-termini of these two receptors govern their association with β-arrestins and the ultimate consequences of scaffolding complex formation, we created chimeras in which the N-terminus of PAR-2 was fused to the C-terminus of NK1R and vice versa. Using subcellular fractionation and confocal microscopy to determine ERK1/2 localization, calcium mobilization assays to determine signal duration, and cell migration and proliferation assays, we show that swapping the C-termini results in a PAR-2-like response to NK1R agonists and an NK1R-like response to PAR-2 agonists, suggesting that the C-termini of the receptors are sufficient to direct specific β-arrestin signaling events." @default.
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- W76819147 date "2007-01-01" @default.
- W76819147 modified "2023-10-16" @default.
- W76819147 title "Interchanging the C‐termini of PAR‐2 and NK1R leads to specific β‐arrestin signaling events" @default.
- W76819147 doi "https://doi.org/10.1096/fasebj.21.6.a982-c" @default.
- W76819147 hasPublicationYear "2007" @default.
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