title: RIP1 comes back to life as a cell death regulator in TNFR1 signaling.
abstract: Cell death induction by tumor necrosis factor has been an intensively studied area for the last two decades. Although it may appear that the skeleton should have been picked clean by now, new secrets about tumor necrosis factor death signaling are still being uncovered. In particular, the recent evidence that ubiquitination of the death kinase receptor-interacting protein 1 regulates its participation in apoptotic and necrotic cell death is opening up unexplored avenues in the catacombs of tumor necrosis factor death signaling. In this minireview, we focus on two major cell-death checkpoints that determine whether receptor-interacting protein 1 functions as a pro-survival or pro-death molecule.
authors.affiliation: Immunology Institute, Mount Sinai School of Medicine, New York, NY 10029, USA. marie.a.odonnell@mssm.edu
authors.forename: Marie Anne
authors.initials: MA
authors.lastname: O'Donnell
authors.forename: Adrian T
authors.initials: AT
authors.lastname: Ting
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000502:physiology; D016923:Cell Death / Q000187:drug effects; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D009336:Necrosis; D053422:Receptor-Interacting Protein Serine-Threonine Kinases / Q000502:physiology; D047888:Receptors, Tumor Necrosis Factor, Type I / Q000502:physiology*; D015398:Signal Transduction; D047992:TNF Receptor-Associated Factor 2 / Q000502:physiology
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; C514981:NEMO protein, mouse; D047888:Receptors, Tumor Necrosis Factor, Type I; D047992:TNF Receptor-Associated Factor 2; C506249:RIPK1 protein, human; D053422:Receptor-Interacting Protein Serine-Threonine Kinases