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• W3140830862 abstract "Macrophages are fundamental for initiation, maintenance, and resolution of inflammation. They can be activated by ‘Toll-like receptor’ (TLR) engagement, which initiates critical pathways to fight infections. ‘Interleukin receptor-associated kinase 2′ (IRAK2) is part of the membrane-proximal Myddosome formed at IL-1R/TLRs, but utility and regulation of IRAK2 within is not completely understood. In this study, we addressed the importance of the evolutionary conserved extreme C-terminus of IRAK2 in TLR signaling. The last 55 amino acids lack any known functional domain. The C-terminus deletion mutant IRAK2Δ55 was hypofunctional and disabled to conduct TLR4-inducible NF-κB and ERK2 activation. Accordingly, it could neither fully support subsequent CD40 cell surface expression nor IL-6 and nitric oxide release. Interestingly, IRAK2Δ55 was still capable to bind to ‘tumor necrosis factor receptor-associated factor 6′ (TRAF6), which is requisite to activate TRAF6 as an E3-ubiquitin ligase for further downstream signaling. However, IRAK-dependent auto-ubiquitination of TRAF6 was impaired, when IRAK2Δ55 was bound. Thus, the conserved last 55 amino acids enable IRAK2 to sustain an optimal TLR response. This knowledge might spark ideas how overshooting inflammatory responses could be modified without blocking the entire immune response." @default.
• W3140830862 created "2021-04-13" @default.
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• W3140830862 date "2021-06-01" @default.
• W3140830862 modified "2023-10-16" @default.
• W3140830862 title "The extreme C-terminus of IRAK2 assures full TRAF6 ubiquitination and optimal TLR signaling" @default.
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• W3140830862 doi "https://doi.org/10.1016/j.molimm.2021.03.022" @default.
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