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Fig 6 (A) Schematic representation of full-length TMEM33 and its mutants. (B-D) The first and the second TM regions of TMEM33 are necessary for its association with MAVS, TBK1, and MITA. HEK 293T cells seeded in 10 cm2 dishes were co-transfected with the indicated plasmids (5 ?g each). After 24 h, cell lysates were immunoprecipitated (IP) with anti-Flag affinity gel (B and C) or anti-Myc affinity gel (D). Then the immunoprecipitates and WCLs were analyzed by IB with the indicated Abs. (E-G) Diagrammatic representations of full-length MAVS/TBK1/MITA and deletion mutants in this study. (H) The N-terminal CARD domain and C-terminal TM domain of MAVS are responsible to its interaction with TMEM33. The experiments were performed similarly as described above for panel B. (I) The N-terminal kinase domain of TBK1 is essential to its interaction with TMEM33. The experiments were performed similarly as described above for panel B. (J) TMEM33 associates with MITA via its N terminus. The experiments were performed similarly as described above for panel B. All experiments were repeated for at least three times with similar results.