MyD88 oligomerization within the complex of activated TLR 7/8 or 9 : MyD88

Stable Identifier
R-HSA-975098
Type
Reaction [binding]
Species
Homo sapiens
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Structural analysis of MyD88:IRAK4 and MyD88:IRAK4:IRAK2 suggested that upon MyD88 recruitment to an activated dimerized TLR the MyD88 death domains clustering induces the formation of Mydosome, a large oligomeric signaling platform (Motshwene PG et al 2009, Lin SC et al 2010). Assembly of these Myddosome complexes brings the kinase domains of IRAKs into proximity for phosphorylation and activation. The oligomer complex stoichiometry was reported as 7:4 and 8:4 for MyD88:IRAK4 (Motshwene PG et al 2009), and 6:4:4 in the complex of MyD88:IRAK4:IRAK2(Lin SC et al 2010).

Literature References
PubMed ID Title Journal Year
20966070 Two human MYD88 variants, S34Y and R98C, interfere with MyD88-IRAK4-myddosome assembly

George, J, Motshwene, PG, Wang, H, Kubarenko, AV, Rautanen, A, Mills, TC, Hill, AV, Gay, NJ, Weber, AN

J. Biol. Chem. 2011
20485341 Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling

Lin, SC, Lo, YC, Wu, H

Nature 2010
19592493 An oligomeric signaling platform formed by the Toll-like receptor signal transducers MyD88 and IRAK-4

Motshwene, PG, Moncrieffe, MC, Grossmann, JG, Kao, C, Ayaluru, M, Sandercock, AM, Robinson, CV, Latz, E, Gay, NJ

J Biol Chem 2009
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