RIP3 Induces Apoptosis Independent of Pronecrotic Kinase Activity
نویسندگان
چکیده
منابع مشابه
Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation
Programmed necrosis is a form of caspase-independent cell death whose molecular regulation is poorly understood. The kinase RIP1 is crucial for programmed necrosis, but also mediates activation of the prosurvival transcription factor NF-kappaB. We postulated that additional molecules are required to specifically activate programmed necrosis. Using a RNA interference screen, we identified the ki...
متن کاملRIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition.
The pronecrotic kinase, receptor interacting protein (RIP1, also called RIPK1) mediates programmed necrosis and, together with its partner, RIP3 (RIPK3), drives midgestational death of caspase 8 (Casp8)-deficient embryos. RIP1 controls a second vital step in mammalian development immediately after birth, the mechanism of which remains unresolved. Rip1(-/-) mice display perinatal lethality, acco...
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Dysregulation of apoptosis is associated with the development of human cancer and resistance to anticancer therapy. The ultimate goal of cancer treatment is to selectively induce cancer cell death and overcome drug resistance. A deeper understanding of how a given chemotherapy affects tumor cell death is needed to develop strategically designed anticancer agents. Here, we use a xenograft mouse ...
متن کاملIdentification of RIP3, a RIP-like kinase that activates apoptosis and NFκB
The tumor necrosis factor receptor 1 (TNFR1) and the Fas receptor recruit complexes formed by the interactions between RIP kinase, TRADD, FADD and RAIDD — adaptor proteins that contain death domains – which in turn recruit other proteins to initiate signaling [1–5]. To identify proteins associated with the TNF signaling pathway, we performed a yeast twohybrid interaction screen using RIP as bai...
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The receptor-interacting protein kinase 3 (RIP3/RIPK3) has emerged as a critical regulator of programmed necrosis/necroptosis, an inflammatory form of cell death with important functions in pathogen-induced and sterile inflammation. RIP3 activation is tightly regulated by phosphorylation, ubiquitination, and caspase-mediated cleavage. These post-translational modifications coordinately regulate...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 2014
ISSN: 1097-2765
DOI: 10.1016/j.molcel.2014.10.021