Reactome | Hyperphosphorylated IRAK1, still within the receptor complex...

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created	[InstanceEdit:446872] Jupe, S, 2009-11-18
dbId	446863
displayName	Hyperphosphorylated IRAK1, still within the receptor complex...
literatureReference	[LiteratureReference:446876] TRAF6 is a signal transducer for interleukin-1 [LiteratureReference:450122] IL-1-induced NFkappa B and c-Jun N-terminal kinase (JNK) activation diverge at IL-1 receptor-associated kinase (IRAK) [LiteratureReference:450115] TRAF6 distinctively mediates MyD88- and IRAK-1-induced activation of NF-kappaB [LiteratureReference:450151] Distinct molecular mechanism for initiating TRAF6 signalling
modified	[InstanceEdit:2262780] Shamovsky, V, 2012-05-21
schemaClass	Summation
text	Hyperphosphorylated IRAK1, still within the receptor complex, binds TRAF6 through multiple regions including the death domain, the undefined domain and the C-terminal C1 domain (Li et al. 2001). The C-terminal region of IRAK-1 contains three potential TRAF6-binding sites; mutation of the amino acids (Glu544, Glu587, Glu706) in these sites to alanine greatly reduces activation of NFkappaB (Ye et al. 2002).

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