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- W2788004032 abstract "Tumor necrosis factor (TNF) can drive inflammation, cell survival, and death. While ubiquitylation-, phosphorylation-, and nuclear factor κB (NF-κB)-dependent checkpoints suppress the cytotoxic potential of TNF, it remains unclear whether ubiquitylation can directly repress TNF-induced death. Here, we show that ubiquitylation regulates RIPK1’s cytotoxic potential not only via activation of downstream kinases and NF-kB transcriptional responses, but also by directly repressing RIPK1 kinase activity via ubiquitin-dependent inactivation. We find that the ubiquitin-associated (UBA) domain of cellular inhibitor of apoptosis (cIAP)1 is required for optimal ubiquitin-lysine occupancy and K48 ubiquitylation of RIPK1. Independently of IKK and MK2, cIAP1-mediated and UBA-assisted ubiquitylation suppresses RIPK1 kinase auto-activation and, in addition, marks it for proteasomal degradation. In the absence of a functional UBA domain of cIAP1, more active RIPK1 kinase accumulates in response to TNF, causing RIPK1 kinase-mediated cell death and systemic inflammatory response syndrome. These results reveal a direct role for cIAP-mediated ubiquitylation in controlling RIPK1 kinase activity and preventing TNF-mediated cytotoxicity." @default.
- W2788004032 created "2018-03-06" @default.
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- W2788004032 date "2018-02-01" @default.
- W2788004032 modified "2023-10-18" @default.
- W2788004032 title "Ubiquitin-Mediated Regulation of RIPK1 Kinase Activity Independent of IKK and MK2" @default.
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- W2788004032 doi "https://doi.org/10.1016/j.molcel.2018.01.027" @default.
- W2788004032 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5823975" @default.
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