Editorial: Community series in targeting signalling pathways in inflammatory diseases, volume II
Abstract
of the conserved BB loop responsible for signal complex assembly and stabilization (4). TIRAP is a 221 amino acid long protein, which is structured into two main domains namely an Nterminal phosphatidylinositol 4,5-bisphosphate (PIP2) binding domain (PBD) and a C-terminal Toll/interleukin-1 receptor (TIR) domain. TIRAP's positioning is mediated by Phosphatidylinositol 4-Phosphate 5-Kinase α (PIP5Kα), which generates PIP2, a crucial lipid that serves as a docking site for TIRAP (5)(6). TIRAP's TIR domain displays structural differences in contrast to the canonic TIR domains. It comprises an extended AB loop that links αA and αB that are developed due to the absence of αB helix classically situated between βB and βC strands (3). These unique structural characteristics of TIRAP have significant implications for immune signaling, as they influence its interactions with other signaling molecules.Consequently, strategies that target and modulate TIRAP-mediated signaling pathways hold promise for the treatment of diseases associated with dysregulated TIR-driven inflammatory responses(3) (7). For example, aberrant TIRAP signaling has been implicated in the pathogenesis of rheumatoid arthritis, where it contributes to destructive inflammation by promoting cytokine production and immune cell activation within affected joints (9).Mechanistically, TIRAP is known to be activated via a post-translation modification i.e. phosphorylation by kinases namely BTK and PKCδ. Expanding TIR domain…
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