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- W2318945295 abstract "Tumor necrosis factor (TNF) is an important mediator that triggers onset of autoimmune diseases and exerts its biological effects by interacting through two types of receptors, TNFR1 and TNFR2. The TNFR2 signaling has significant potential to exert pro-survival and protective roles in several disorders. Unlike TNFR1 signaling, however, the mechanism of TNFR2 signal transduction is poorly understood, and few of its adapter molecules are known. The present study utilized a proteomics approach to search for adapter molecules in the TNFR2 signaling complex and identified aminopeptidase P3 (APP3) to be a key molecule. One of its two isoforms, mitochondrial APP3 (APP3m) but not cytosolic APP3 (APP3c), was recruited to TNFR2 and shown to regulate TNF/TNFR2-dependent JNK phosphorylation. Furthermore, APP3m was released from mitochondria upon TNF stimulation in the absence of mitochondrial outer membrane permeabilization (MOMP). The observation of increased cell death by down-regulation of APP3m also suggested that APP3m exerts an anti-apoptotic function. These findings reveal that APP3m is a new member of the TNF/TNFR2 signaling complex and characterize an APP3-mediated TNFR2 signal transduction mechanism that induces JNK activation." @default.
- W2318945295 created "2016-06-24" @default.
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- W2318945295 date "2015-01-01" @default.
- W2318945295 modified "2023-10-10" @default.
- W2318945295 title "Aminopeptidase P3 (APP3), a novel member of the TNF/TNFR2 signaling complex, induces phosphorylation of JNK" @default.
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- W2318945295 doi "https://doi.org/10.1242/jcs.149385" @default.
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