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. Author manuscript; available in PMC: 2015 Oct 13.
Published in final edited form as: Cell Res. 2009 Feb;19(2):208–215. doi: 10.1038/cr.2008.320

Figure 1.

Figure 1

IL-17RD interacts with IL-17R. (A) IL-17R-Myc and IL-17RD-Flag interact in HEK293T cells. HEK293T cells were transfected with the indicated plasmids for 24 h, treated with 100 ng/ml IL-17 for the indicated time, then lysed and immunoprecipitated with Flag antibody and Protein G PLUS-Agarose beads. Top panel, Flag immunoprecipitates were resolved by SDS-PAGE and blotted with anti-Myc antibody to detect co-precipitated IL-17R. Center panel and bottom panel, whole cell lysates (WCL) of transfected cells were blotted with anti-Myc and anti-Flag antibodies to determine the expression levels of the IL-17R and IL-17RD proteins, respectively. (B) Interaction of endogenous IL-17R and IL-17RD. MEF and NIH3T3 cells treated with or without IL-17 stimulation were used to immunoprecipitate complexes after lysis. Anti-IL-17R and IL-17RD antibodies were used for immunoprecipitation and western blot analysis. 5% of the cell lysates were used for the input. (C) IL-17RD interacts with both IL-17R-Myc and IL-17RB-Myc. Immunoprecipitations were carried out using anti-IL-17RD rabbit polyclonal antibodies and protein G PLUS-Agarose beads and subjected to immunoblotting with anti-Myc antibody. (D) Both the intracellular and extra-cellular domains of IL-17RD interact with IL-17R. Immunoprecipitations were carried out using anti-Myc antibody and protein G PLUS-Agarose beads and subjected to immunoblotting with anti-HA antibody. IL-17RDΔECD represents the deletion of the extracellular domain of IL-17RD, and IL-17RDΔICD represents the deletion of the intracellular domain.