ArticleBiochemistry2014
Structural study of the RIPoptosome core reveals a helical assembly for kinase recruitment.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Article
- For Better or Worse: The Impact of Necrotic Cell Death Modalities.Advances in experimental medicine and biology · 2025Review
- The interaction between RIPK1 and FADD controls perinatal lethality and inflammation.Cell reports · 2024Article
- Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation.International journal of molecular sciences · 2024Review
- Bioluminescent RIPoptosome Assay for FADD/RIPK1 Interaction Based on Split Luciferase Assay in a Human Neuroblastoma Cell Line SH-SY5Y.Biosensors · 2023Article
- Amyloid-like RIP1/RIP3 RHIM Fragments' Characterization and Application as a Drug Depot.Molecules (Basel, Switzerland) · 2023Article
- ANKRD13a controls early cell-death checkpoint by interacting with RIP1 independent of NF-κB.Cell death and differentiation · 2022Article
- Supramolecular organizing centers at the interface of inflammation and neurodegeneration.Frontiers in immunology · 2022Review
- Detecting Necroptosis in Virus-Infected Cells.Methods in molecular biology (Clifton, N.J.) · 2021Article
- From pyroptosis, apoptosis and necroptosis to PANoptosis: A mechanistic compendium of programmed cell death pathways.Computational and structural biotechnology journal · 2021Review
- Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.Experimental & molecular medicine · 2020Review
- Heterogeneous responses to low level death receptor activation are explained by random molecular assembly of the Caspase-8 activation platform.PLoS computational biology · 2019Article
- Identification and analysis of dominant negative mutants of RIP1 DD that disrupt RIPoptosome core formation.Molecular biology reports · 2018Article
- RIP2 filament formation is required for NOD2 dependent NF-κB signalling.Nature communications · 2018Article
- Review
- Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex.Molecular cell · 2016Article
- Rescuing neuronal cell death by RAIDD- and PIDD- derived peptides and its implications for therapeutic intervention in neurodegenerative diseases.Scientific reports · 2016Article
- Absence of RIPK3 predicts necroptosis resistance in malignant melanoma.Cell death & disease · 2015Article
- Article
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Authors and funding
8 authors.
Funding
Abstract
Receptor interaction protein kinase 1 (RIP1) is a molecular cell-fate switch. RIP1, together with Fas-associated protein with death domain (FADD) and caspase-8, forms the RIPoptosome that activates apoptosis. RIP1 also associates with RIP3 to form the necrosome that triggers necroptosis. The RIPoptosome assembles through interactions between the death domains (DDs) of RIP1 and FADD and between death effector domains (DEDs) of FADD and caspase-8. In this study, we analyzed the overall structure of the RIP1 DD/FADD DD complex, the core of the RIPoptosome, by negative-stain electron microscopy and modeling. The results show that RIP1 DD and FADD DD form a stable complex in vitro similar to the previously described Fas DD/FADD DD complex, suggesting that the RIPoptosome and the Fas death-inducing signaling complex share a common assembly mechanism. Both complexes adopt a helical conformation that requires type I, II, and III interactions between the death domains.
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Registered trials
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