Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death

Article Abstract:

Tumor necrosis factor (TNF) elicits cellular responses to inflammation and infection by activating cell surface receptors such as TNFR1. Analysis of the mechanism of TNFR1 activity using the protein recruitment model for TNFR1 signaling showed that TNFR1 utilize distinct, separate pathways. TNFR1 activates apoptosis by recruiting the signal transducer FADD to the TNFR1 complex. On the other hand, JNK and NF-kappabeta activation require the signal transducers RIP and TRAF2.

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Reactive oxygen species promote TNF alpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases

Article Abstract:

The Tumor Necrosis factor (TNFalpha) is a pleiotropic cytokine that induces either cell proliferation or cell death and the inhibition of Necrosis Factor-kappaB activation increases susceptibility to Tumor Necrosis Factor alpha-induced death concurrent with sustained Jun N-terminal Kinase activation. Intracellular H2O2 accumulation inactivates mitogen activated protein kinases by oxidation of their catalytic cysteine.

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The E3 ubiquitin ligase itch couples JNK activation to TNF alpha-induced cell death by inducing c-FLIP turnover

Article Abstract:

The turnover of the NF-KB-induced antiapoptotic protein C-FLIP is accelerated by tumor necrosis factor (TNF) alpha-mediated Jun kinase (JNK) activation. JNK promotes the proteasomal elimination of c-FLIP and thus antagonizes NF-KB during TNF alpha signaling.

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