Dissociation of hp-IRAK1:TRAF6 or IRAK2:TRAF6-oligomer from the activated TLR5 or 10:oligo-Myd88:p-IRAK4 complex

Stable Identifier
Reaction [dissociation]
Homo sapiens
Related Species
Escherichia coli
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Hyperphosphorylated IRAK1 and TRAF6 are thought to dissociate from the activated receptor. (Gottipati et al. 2007) but the IRAK1:TRAF6 complex may remain associated with the membrane (Dong et al. 2006).

Phosphorylated IRAK2, like its paralog IRAK1, possibly dissociates from the activated receptor as shown here, although mechanism of IRAK2 activation by IRAK4 followed by TRAF6 binding remains to be deciphered.

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

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

Cell Signal 2008
14625308 Sequential autophosphorylation steps in the interleukin-1 Receptor-associated Kinase-1 Regulate its Availability as an Adapter in Interleukin-1 Signaling

Kollewe, C, Mackensen, AC, Neumann, D, Knop, J, Cao, P, Li, S, Wesche, H, Martin, MU

J Biol Chem 2004
Participant Of
Cite Us!