TRAF6 binding leads to IRAK1:TRAF6 release

Stable Identifier
Reaction [dissociation]
Homo sapiens
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MyD88 and Tollip only bind to non-phosphorylated IRAK1 (Wesche et al. 1997) so hyper-phosphorylated IRAK1 is predisposed to release from the receptor complex, a key step in this signaling cascade. It is believed that the interaction of IRAK1 with TRAF6 enables the release of IRAK1:TRAF6 from the receptor (Gottipati et al. 2007). Though released from the receptor complex, IRAK1:TRAF6 remains associated with the membrane, perhaps due to subsequent interaction with the TAK1 complex (Dong et al. 2006). Interleukin-1 receptor-associated kinase 3 (IRAK3 or IRAK-M) prevents the dissociation of IRAK1 and IRAK4 from the MYD88 oligomeric signaling complex called the Myddosome (Kobayashi K et al. 2002).

Literature References
PubMed ID Title Journal Year
17890055 IRAK1: a critical signaling mediator of innate immunity

Rao, NL, Gottipati, S, Fung-Leung, WP

Cell Signal 2008
This event is regulated
Negatively by