Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis.
Caspases play a central role in the execution phase of apoptosis and are responsible for many of the morphological features normally associated with this form of cell death. Caspases can activate one another and consequently can initiate specific caspase cascades. Caspases-8 and -9 appear to be the apical caspases activated in death receptor- and mitochondrial stress-induced apoptosis, respectively. The role of large protein complexes in mediating these pathways is discussed.
Bratton
S B
SB
MRC Toxicology Unit, Hodgkin Building, University of Leicester, Lancaster Road, Leicester, LE1 9HN, United Kingdom.
MacFarlane
M
M
Cain
K
K
Cohen
G M
GM
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000502:physiology; D053220:Receptors, TNF-Related Apoptosis-Inducing Ligand; D018124:Receptors, Tumor Necrosis Factor / Q000502:physiology; D015398:Signal Transduction
D053220:Receptors, TNF-Related Apoptosis-Inducing Ligand; D018124:Receptors, Tumor Necrosis Factor; C105190:TNFRSF10A protein, human; C505639:TNFRSF10B protein, human; C505530:CASP8 protein, human; C506433:CASP9 protein, human; D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases