Supplementary Materials

This PDF file includes:

  • Fig. S1. Properties of N-glycosylation–deficient HA-BLT1/0N.
  • Fig. S2. Conserved Ser and Thr residues in the cytoplasmic domains of human, mouse, rat, guinea pig, and zebrafish BLT1.
  • Fig. S3. Confirmation of residues essential for HA-BLT1/0N phosphorylation.
  • Fig. S4. Phosphorylation of mouse BLT1.
  • Fig. S5. Phosphorylation at LTB4-induced and basal sites through Gi.
  • Fig. S6. LTB4 dose dependency of intracellular [Ca2+] increase.
  • Fig. S7. Effect of blockage of the [Ca2+] increase on BLT1 phosphorylation.
  • Fig. S8. Effect of phosphorylation deficiency on the functions of wild-type BLT1.
  • Fig. S9. Effect of helix 8 disruption on BLT1 phosphorylation.
  • Fig. S10. Importance of phosphorylation for the ligand sensitivity of BLT1.
  • Fig. S11. Effect of phosphorylation on β-arrestin binding to BLT1.
  • Table S1. Primer sequences used to generate mutant BLT1s.

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