AIP1 mediates TNF-α–induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3
J. Clin. Invest. Rong Zhang, et al. 111:1933 doi:10.1172/JCI17790 [Go to this article.]

Figure 1
The C2 domain of AIP1 is critical for ASK1 binding. (a) Schematic diagram of AIP1 domains and expression constructs. The full-length AIP1 (AIP1-F) contains an N-terminal (AIP1-N) and a C-terminal half (AIP1-C). AIP1-N consists of a PH, a C2, and a GAP domain. The C-terminal half contains a proline-rich sequence (PR) and a leucine-zipper motif (LZ). AIP1-PHC2 contains the PH and C2 domains. AIP1-PH contains the PH domain only. AA, amino acid. (b) The C2 domain of AIP1 is critical for ASK1 binding. BAECs were transfected with FLAG-tagged AIP1-N, AIP1-C, AIP1-PHC2, or AIP1-PH, and expression of AIP1 was determined by Western blot with anti-FLAG. Interaction of AIP1 domains with endogenous ASK1 was examined by immunoprecipitation with anti-ASK1, followed by Western blot with anti-FLAG. ASK1 protein in immunoprecipitates was determined by Western blot with anti-ASK1.