Source:http://www.reactome.org/biopax/48887BiochemicalReaction2545
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Authored: Shamovsky, V, 2010-06-01,
Edited: Shamovsky, V, 2010-11-15,
Reviewed: Gillespie, ME, 2010-10-29,
TAK1-binding protein 2 (TAB2) and/or TAB3, as part of a complex that also contains TAK1 and TAB1, binds polyubiquitinated TRAF6. The TAB2 and TAB3 regulatory subunits of the TAK1 complex contain C-terminal nuclear zinc finger motifs that interact with K63-pUb chains (Kanayama et al. 2004). TAK1 can be activated by unattached K63-polyubiquitinated chains when TRAF6 has no detectable polyubiquitination (Xia et al. 2009) and thus the synthesis of these chains by TRAF6 may be the signal transduction mechanism.
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Activated TRAF6:p-IRAK2 interacts with TAK1 complex upon TLR7/8 or 9 stimulation
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