title: Molecular cell death platforms and assemblies.
abstract: Multi-cellular animals have evolved a variety of mechanisms to respond to diverse apoptotic stimuli. In general these proceed through activation of apical caspases and culminate in executioner caspase activation and cell death. Because of the breadth of possible initiators, various molecular platforms are used to trigger different apical caspases. Although some common protein domains are used to assemble the apoptosome, the PIDDosome and death receptor complexes, an array of checks-and-balances are employed to ensure appropriate activation. Notwithstanding, these pathways share the underlying principle of proximity-dependent activation and post-translational modification. Here we will describe our current structural understanding of assembly and regulation of these signaling platforms.
authors.affiliation: Program in Apoptosis and Cell Death Research, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
authors.forename: Peter D
authors.initials: PD
authors.lastname: Mace
authors.forename: Stefan J
authors.initials: SJ
authors.lastname: Riedl
mesh_terms: D000818:Animals; D053478:Apoptosomes / Q000378:metabolism; D020169:Caspases / Q000378:metabolism; D016923:Cell Death; D004789:Enzyme Activation; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / Q000378:metabolism
chemical_list: D053478:Apoptosomes; D047988:Tumor Necrosis Factor Receptor-Associated Peptides and Proteins; D020169:Caspases
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