K-63 linked polyubiquitin (pUb) chain on TRAF6 provides a scaffold to recruit downstream effector molecules to activate NF-kB. Transforming growth factor beta-activated kinase 1 (TAK1) is a member of the mitogen-activated protein kinase (MAPK) kinase kinase family is shown to be an essential intermediate that transmits the upstream signals from the receptor complex to the downstream MAPKs and to the NF-kB pathway (Broglie et al. 2009). TAK1-binding protein 1 (TAB1), TAB2 and TAB3 constitutively bound to TAK1. TAB1 acts as the activation subunit of the TAK1 complex, aiding in the autophosphorylation of TAK1, whereas TAB2 and its homologue TAB3, act as a adaptors of TAK1 that facilitate the assembly of TAK1 complex to TRAF6. The highly conserved C-terminal zinc finger domain of TAB2 and TAB3 binds preferentially to the K-63-linked polyubiquitin chains on TRAF6 (Broglie et al. 2009, Besse et al. 2007).
Kishida, S, Shibuya, H, Takaesu, G, Ninomiya-Tsuji, J, Matsumoto, K, Yamaguchi, K, Hiyama, A, Irie, K
Maddineni, U, Wu, H, Darnay, BG, Lin, SC, Besse, A, Lamothe, B, Campos, AD, Webster, WK
Deng, L, Seth, RB, Kanayama, A, Shaito, A, Hong, M, Chiu, YH, Chen, ZJ, Sun, L, Ea, CK
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