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Clin Immunol ; 238: 108998, 2022 05.
Article in English | MEDLINE | ID: mdl-35398286

ABSTRACT

Deciphering signaling pathways that regulate the complex interplay between inflammation and cell death is a key challenge in understanding innate immune responses. Over recent years, receptor interacting protein (RIP) kinases have been described to regulate the interplay between inflammation and cell death. Whereas RIP1 and 3, the most well described members of the RIP kinase family, play important roles in necroptosis, RIP2's involvement in regulating inflammation, cell death processes and cancer is less well described and controversially discussed. Here, we demonstrate that RIP2 exerts immune regulatory functions by regulating mitochondrial damage and mitochondrial superoxide production in response to SV40 LT-induced genotoxic stress by the induction of ULK1-phosphorylation, therefore regulating the expression of interferon stimulated genes (ISGs) and NLRP3-inflammasome dependent IL-1ß release. Because RIP2 is upregulated and/or activated in autoimmune/inflammatory disease and cancer, observations from this study promise implications of RIP kinases in human disease.


Subject(s)
Inflammation , Receptor-Interacting Protein Serine-Threonine Kinase 2 , DNA Damage , Homeostasis , Humans , Reactive Oxygen Species/metabolism , Receptor-Interacting Protein Serine-Threonine Kinase 2/metabolism
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