Recruitment of TRAF6 to CBM complex by binding to MALT1

Stable Identifier
Reaction [binding]
Homo sapiens
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TRAF6 is a ubiquitin ligase that plays a central role in the IKK-dependent canonical NF-kB pathway. It is recruited to the CBM complex by binding to MALT1. The MALT1 C-terminal Ig domain and extension contain two binding motifs for TRAF6 (Noels et al 2007). After oligomerzation TRAF6, together with Ubc13/Uev1A, activates TAK1 and IKK. It also acts as an E3 ligase for MALT1 and mediates lysine 63-linked ubiquitination (Oeckinghaus et al. 2007).

Literature References
PubMed ID Title Journal Year
17948050 Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation

Oeckinghaus, A, Wegener, E, Welteke, V, Ferch, U, Arslan, SC, Ruland, J, Scheidereit, C, Krappmann, D

EMBO J. 2007
18772140 TRAF6 specifically contributes to FcepsilonRI-mediated cytokine production but not mast cell degranulation

Yang, YJ, Chen, W, Carrigan, SO, Chen, WM, Roth, K, Akiyama, T, Inoue, J, Marshall, JS, Berman, JN, Lin, TJ

J. Biol. Chem. 2008
Participant Of
Orthologous Events
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