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• W1996581446 abstract "Tumor necrosis factor receptor (TNFR) superfamily members can induce a context-dependent apoptosis or cell activation. However, the mechanisms by which these opposing programs are selected remain unclear. We show that in T cells, TNFR2 (TNFRSF1B) signaling is dramatically affected by the intracellular mediator RIP, a protein Ser/Thr kinase required for NF-kappaB activation by TNFR1 (TNFRSF1A). In the presence of RIP, TNFR2 triggers cell death, whereas in the absence of RIP, TNFR2 activates NF-kappaB. RIP is induced during IL2-driven T cell proliferation, and its inhibition reduces susceptibility to TNF-dependent apoptosis. Evidence that signaling outputs are shaped by intracellular constraints helps reconcile conflicting views of TNFR1 and TNFR2 as apoptotic mediators." @default.
• W1996581446 created "2016-06-24" @default.
• W1996581446 creator A5038604609 @default.
• W1996581446 creator A5090399098 @default.
• W1996581446 date "1999-12-01" @default.
• W1996581446 modified "2023-09-27" @default.
• W1996581446 title "Regulated Commitment of TNF Receptor Signaling" @default.
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• W1996581446 doi "https://doi.org/10.1016/s1074-7613(00)80152-1" @default.
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