Dissociation of hp-IRAK1/or IRAK2:TRAF6-oligomer from the p-IRAK4 :oligo-Myd88:activated TLR7/8 or 9 complex

Stable Identifier
R-HSA-975100
Type
Reaction [dissociation]
Species
Homo sapiens
Related Species
Human immunodeficiency virus 1, Influenza A virus, Human SARS coronavirus, Severe acute respiratory syndrome coronavirus 2
Compartment
endosome membrane
ReviewStatus
5/5
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Dissociation of hp-IRAK1/or IRAK2:TRAF6-oligomer from the p-IRAK4 :oligo-Myd88:activated TLR7/8 or 9 complex
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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
Participants
Input
Output
Participates
as an event of
Orthologous Events
p-IRAK2- TRAF6 dissociates from the activated TRL7 or 21 (Gallus gallus)
Authored
de Bono, B  (2005-08-16)
Reviewed
Gillespie, ME  (2010-10-29)
Created
Shamovsky, V  (2010-09-22)
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