Figure 2.

Schematic illustrations of ASK1 and ASK2. The domain structures of ASK1 and ASK2 are illustrated. The binding domains of Trx and TRAF exist in the N-terminus of ASK1. Two coiled-coil domains (NCC and CCC) are important for the homomeric interaction and the activation of ASK1. ASK2 associates with the ASK1 C-terminus, which is required to stabilize the ASK2 protein. In the lower part, highly conserved amino acid sequences around the activation loop of the kinase domains of the ASK family are aligned with orthologues of invertebrate ASK1 (DASK1: D. melanogaster, NSY-1: C. elegans). A phosphorylation site essential for ASK1 activation (Thr845 in mouse-ASK1) is shown in red and by a star (*). Three autophosphorylation sites identified in ASK1 are enclosed in squares.