TRAF2:cIAP1/2 complex binds FN14:TWEAK

Stable Identifier
Reaction [binding]
Homo sapiens
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The FN14 (TNFRSF12A) intracellular domain lacks the characteristic death domain of TNF receptor superfamily (TNFRSF) but contains TNFR-associated factor (TRAF) binding sites. Upon TWEAK binding, FN14 recruits TRAF2 and TRAF3 to activate both canonical and non-canonical nuclear factor-kappa B (NF-kB) pathway (Brown et al. 2003, Saitoh et al. 2003, Sanz et al. 2010). NF-kB activation plays a key role in TWEAK-elicited inflammatory responses. TWEAK/FN14 binding induces NIK activation through targeting the degradation of TRAF2/cellular inhibitor of apoptosis (cIAP) 1 and 2 complex (Vince et al. 2008). TWEAK activation of the non-canonical NF-kB pathways promotes inflammatory responses in tubular cells. In cultured renal tubular cells TWEAK increases nuclear RelB/p52 accumulation, RelB and p52 DNA-binding activity, and NIK- and RelB-dependent CCL21 and CCL19 expression (Poveda et al. 2010).

Literature References
PubMed ID Title Journal Year
12529173 The Fn14 cytoplasmic tail binds tumour-necrosis-factor-receptor-associated factors 1, 2, 3 and 5 and mediates nuclear factor-kappaB activation

Richards, CM, Feng, SL, Winkles, JA, Brown, SA, Hanscom, HN

Biochem. J. 2003
Orthologous Events
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