Unknown

Dataset Information

0

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.

SUBMITTER: Mace PD 

PROVIDER: S-EPMC2993832 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Molecular cell death platforms and assemblies.

Mace Peter D PD   Riedl Stefan J SJ  

Current opinion in cell biology 20101201 6


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  ...[more]

Similar Datasets

| S-BSST17 | biostudies-other
| S-EPMC9829448 | biostudies-literature
| S-EPMC5479803 | biostudies-literature
| S-EPMC6070399 | biostudies-literature
| S-EPMC4064824 | biostudies-literature
| S-EPMC2174518 | biostudies-literature
| S-EPMC5864239 | biostudies-literature
| S-EPMC5972272 | biostudies-literature
| S-EPMC4961660 | biostudies-literature
| S-EPMC3612676 | biostudies-other