TRAF6 binding to activated IRAK2 stimulates its oligomerization

Stable Identifier
R-GGA-451466
Type
Reaction [binding]
Species
Gallus gallus
Compartment
cytosol, plasma membrane
ReviewStatus
5/5
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TRAF6 binding to activated IRAK2 stimulates its oligomerization
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There is little experimental data about mammalian IRAK2 mediated signaling. It is possible that phosphorylated IRAK2, like IRAK1, dissociates from upstream adapters such as MyD88 but leaves its interaction with the downstream adapter TRAF6 unaffected. Furthermore Keating et al. [2007] showed that IRAK2 can promote TRAF6 ubiquitination. Other studies [Wan et al 2009] detected IRAK2-TRAF6 interaction upon LPS stimulation.

In this reaction we assume that chicken IRAK2 behaves like its mammalian homolog IRAK2.

Literature References
PubMed ID Title Journal Year
18070982 TRAF6 distinctively mediates MyD88- and IRAK-1-induced activation of NF-kappaB

Muroi, M, Tanamoto, K

J Leukoc Biol 2008
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Inferred From
IRAK2 induces TRAF6 oligomerization (Homo sapiens)
Authored
Shamovsky, V  (2010-01-05)
Reviewed
D'Eustachio, P  (2010-10-16)
Created
Shamovsky, V  (2010-01-05)
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