EMBO J. 1996 Nov 15;15(22):6189-96.

RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis.

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Department of Molecular Biology, Massachusetts General Hospital, Boston 02114, USA.

Abstract

The CD95 (Fas/APO-1) and tumor necrosis factor (TNF) receptor pathways share many similarities, including a common reliance on proteins containing 'death domains' for elements of the membrane-proximal signal relay. We have created mutant cell lines that are unable to activate NF-kappaB in response to TNF. One of the mutant lines lacks RIP, a 74 kDa Ser/Thr kinase originally identified by its ability to associate with Fas/APO-1 and induce cell death. Reconstitution of the line with RIP restores responsiveness to TNF. The RIP-deficient cell line is susceptible to apoptosis initiated by anti-CD95 antibodies. An analysis of cells reconstituted with mutant forms of RIP reveals similarities between the action of RIP and FADD/MORT-1, a Fas-associated death domain protein.

PMID:: 8947041; [PubMed - indexed for MEDLINE]
PMCID: PMC452440

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DK43031/DK/NIDDK NIH HHS/United States

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anti-Receptor-Interacting Serine threonine-Protein Kinase 1 (RIPK1) antibody - antibodies-online

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