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• W4383302647 abstract "Toll-interacting protein (Tollip) is a multifunctional regulator in cellular activities. However, whether its functions are subjected to post-translational modifications remains elusive. Here, we identified ubiquitination as a post-translational modification on Tollip. We found that Tollip interacted with ring finger protein 167 (RNF167) through its C-terminal coupling of ubiquitin to ER degradation (CUE) domain, and RNF167 functioned as the potential E3 ligase to attach K33-linked poly-ubiquitin chains to the Lys235 (K235) site of Tollip. Furthermore, we discovered Tollip could inhibit TNF-α-induced nuclear factor-kappa B (NF-κB) and mitogen-activated protein kinase (MAPK) activation, and substitution of Lys235 on Tollip to arginine failed to suppress TNF-α-NF-κB/MAPK (JNK) cascades, revealing the role of Tollip and its ubiquitination in NF-κB/MAPK pathways. Thus, our study reveals the novel biological function of Tollip and RNF167-dependent ubiquitination of Tollip in TNF-α signaling." @default.
• W4383302647 created "2023-07-07" @default.
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• W4383302647 date "2023-07-06" @default.
• W4383302647 modified "2023-10-17" @default.
• W4383302647 title "<scp>RNF167</scp>‐mediated ubiquitination of Tollip inhibits <scp>TNF‐α</scp>‐triggered <scp>NF‐κB</scp> and <scp>MAPK</scp> activation" @default.
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• W4383302647 doi "https://doi.org/10.1096/fj.202201839r" @default.
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