Article Figures & Data
Additional Files
Data Supplement
- Supplemental Data -
Supplemental Fig. 1. Genomic sequence of β-arrestin-2 mutant BEAS-2B cells.
Supplemental Fig. 2. Salmeterol promotes ERK1/2 phosphorylation in HEK293β2 cells by a β2-adrenoceptor-mediated mechanism.
Supplemental Fig. 3. Salmeterol promotes ERK1/2 dephosphorylation in BEAS-2B cells.
Supplemental Fig. 4. Salmeterol and indacaterol promote ERK1/2 dephosphorylation in HBEC by a β2-adrenoceptor-mediated mechanism.
Supplemental Fig. 5. Salmeterol promotes ERK1/2 dephosphorylation in airway epithelial cells in a PKA-dependent manner.
Supplemental Fig. 6. Effects of EGF on the phosphorylation status of C-Raf, MEK1/2 and ERK1/2 in BEAS-2B cells.
Supplemental Fig. 7. Antagonism of carvedilol-, alprenolol- and carazolol-induced ERK1/2 phosphorylation in HEK293β2 cells by ICI 118,551.
Supplemental Fig. 8. Identification of β-arrestin 1 by western blotting.
Supplemental Fig. 9. Confirmation of ARRB2 knockout in clonal BEAS-2B cells and the impact on formoterol-induced ERK1/2 dephosphorylation.
Supplemental Fig. 10. Lack of effect of formoterol on the expression of genes in HBEC that are implicated in β2
-adrenoceptor-mediated ERK1/2 phosphorylation in HEK293 and related cell systems.Supplemental Fig. 11. Lack of effect of receptor antagonists and Gq inhibition on basal and EGF-induced ERK1/2 phosphorylation.
- Supplemental Data -