Dissociation of p-IRAK2:TRAF6 from the activated TLR:oligo-Myd88:TIRAP:p-IRAK4 complex

Stable Identifier
R-HSA-2262775
Type
Reaction
Species
Homo sapiens
Related Species
Chlamydia trachomatis, Neisseria meningitidis serogroup B
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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
14625308 Sequential autophosphorylation steps in the interleukin-1 Receptor-associated Kinase-1 Regulate its Availability as an Adapter in Interleukin-1 Signaling

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

J Biol Chem 2004
17890055 IRAK1: a critical signaling mediator of innate immunity

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

Cell Signal 2008
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