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Human Interaction Network Ontology
Last uploaded:
June 27, 2014
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| Id | http://purl.obolibrary.org/obo/HINO_0022346
http://purl.obolibrary.org/obo/HINO_0022346
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|---|---|
| Preferred Name | IRAK2 mediated activation of TAK1 complex |
| Definitions |
Reviewed: Napetschnig, Johanna, 2012-11-16
Although IRAK-1 was originally thought to be a key mediator of TRAF6 activation in the IL1R/TLR signaling (Dong W et al. 2006), recent studies showed that IRAK-2, but not IRAK-1, led to TRAF6 polyubiquitination (Keating SE et al 2007). IRAK-2 loss-of-function mutants, with mutated TRAF6-binding motifs, could no longer activate NF-kB and could no longer stimulate TRAF-6 ubiquitination (Keating SE et al 2007). Furthermore, the proxyvirus protein A52 - an inhibitor of all IL-1R/TLR pathways to NF-kB activation, was found to interact with both IRAK-2 and TRAF6, but not IRAK-1. Further work showed that A52 inhibits IRAK-2 functions, whereas association with TRAF6 results in A52-induced MAPK activation. The strong inhibition effect of A52 was also observed on the TLR3-NFkB axis and this observation led to the discovery that IRAK-2 is recruited to TLR3 to activate NF-kB (Keating SE et al 2007). Thus, A52 possibly inhibits MyD88-independent TLR3 pathways to NF-kB via targeting IRAK-2 as it does for other IL-1R/TLR pathways, although it remains unclear how IRAK-2 is involved in TLR3 signaling.<p>IRAK-2 was shown to have two TRAF6 binding motifs that are responsible for initiating TRAF6 signaling transduction (Ye H et al 2002).
Edited: Shamovsky, V, 2012-11-06
Reviewed: Gillespie, ME, 2010-11-30
Authored: Shamovsky, V, 2010-06-01
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| Type | http://www.w3.org/2002/07/owl#Class |
All Properties
| label |
IRAK2 mediated activation of TAK1 complex
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|---|---|
| comment |
Reviewed: Napetschnig, Johanna, 2012-11-16
Although IRAK-1 was originally thought to be a key mediator of TRAF6 activation in the IL1R/TLR signaling (Dong W et al. 2006), recent studies showed that IRAK-2, but not IRAK-1, led to TRAF6 polyubiquitination (Keating SE et al 2007). IRAK-2 loss-of-function mutants, with mutated TRAF6-binding motifs, could no longer activate NF-kB and could no longer stimulate TRAF-6 ubiquitination (Keating SE et al 2007). Furthermore, the proxyvirus protein A52 - an inhibitor of all IL-1R/TLR pathways to NF-kB activation, was found to interact with both IRAK-2 and TRAF6, but not IRAK-1. Further work showed that A52 inhibits IRAK-2 functions, whereas association with TRAF6 results in A52-induced MAPK activation. The strong inhibition effect of A52 was also observed on the TLR3-NFkB axis and this observation led to the discovery that IRAK-2 is recruited to TLR3 to activate NF-kB (Keating SE et al 2007). Thus, A52 possibly inhibits MyD88-independent TLR3 pathways to NF-kB via targeting IRAK-2 as it does for other IL-1R/TLR pathways, although it remains unclear how IRAK-2 is involved in TLR3 signaling.<p>IRAK-2 was shown to have two TRAF6 binding motifs that are responsible for initiating TRAF6 signaling transduction (Ye H et al 2002).
Edited: Shamovsky, V, 2012-11-06
Reviewed: Gillespie, ME, 2010-11-30
Authored: Shamovsky, V, 2010-06-01
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| prefLabel |
IRAK2 mediated activation of TAK1 complex
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| located_in | |
| definition source |
Pubmed16831874
Pubmed12140561
Reactome, http://www.reactome.org
Pubmed21606490
Pubmed17878161
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| prefixIRI |
HINO:0022346
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| seeAlso |
Reactome Database ID Release 43937042
ReactomeREACT_25380
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| subClassOf | |
| type | |
| has_part |
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