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Fig. 1. RIP2 interacts with TRIP6. (A) The structures of RIP2, TRIP6 and their deletion mutants. The kinase and CARD domains of RIP2 and the LIM domains and nuclear export sequence (NES) of TRIP6 are indicated. (B) TRIP6 interacts with RIP2 and its individual domains. 293 cells (2x10⁶) were transfected with 5 µg each of HA-TRIP6 and Flag-tagged RIP2 or its mutant plasmids. Cell lysates were immunoprecipitated with anti-Flag antibody ( ${alpha}$ -F) or control mouse IgG (C). The immunoprecipitates were analysed by western blot with horseradish-peroxidase (HRP)-conjugated anti-HA antibody (top). Expression of the transfected proteins in the lysates was detected by western blot analysis with anti-Flag (middle) or anti-HA (bottom) antibody. (C) RIP2 interacts with the LIM domains of TRIP6. 293 cells (2x10⁶) were transfected with 5 µg each of Flag-RIP2 and HA-tagged TRIP6 and its mutant plasmids. Cell lysates were immunoprecipitated with anti-Flag antibody ( ${alpha}$ -F) or control mouse IgG (C). The immunoprecipitates and cell lysates (L) were analysed by western blot with a combination of anti-HA and anti-Flag antibodies. (D) RIP2 and TRIP6 interact in untransfected cells in a stimulation-dependent manner. 293 cells (2x10⁷) were treated with TNF (10 ng ml^-1) or IL-1 (10 ng ml^-1), or left untreated for 5 minutes. Cells were lysed and the lysate was immunoprecipitated with goat anti-RIP2 antibody or control goat IgG. The immunoprecipitates were analysed by western blot with rabbit anti-TRIP6 antibody.

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