Figure: signaling pathways: caspases

^[1]^[2]^[3]^[4]

Introduction

Apoptotic pathways which target procaspases to membrane receptors.

cytoplasmic domains of FAS/Apo1 associate with death domains of adaptor molecules FADD, TRADD, RIP & RAIDD
death effector domain in FADD associates with procaspases 8 or 10
procaspase 2 associates with RAIDD in a region homologous to the procaspase 2 prodomain
activated caspase 8 & caspase 10 activate caspase 3
when mitochondrion receive apoptic cue, cytochrome c is released into the cytosol & complexes with Apaf-1 & procaspase 9 to produce active caspase 9 which also activates procaspase 3
after stress to the endoplasmic reticulum, caspase 12 is activated
in addition to cytochrome c, mitochondria also release apoptosis inducing factor (AIF) & procaspases: procaspase 2, procaspase3 & procaspase9 after apoptotic stimuli

↑ Villa P, Kaufmann SH, Earnshaw WC. Caspases and caspase inhibitors. Trends Biochem Sci. 1997 Oct;22(10):388-93. PMID: https://www.ncbi.nlm.nih.gov/pubmed/9357314 Review.
↑ Gervais et al. Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation. Cell 97:395-406, 1999 PMID: https://www.ncbi.nlm.nih.gov/pubmed/10319819 Free article
↑ Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature, 2000;403:98-103 PMID: https://www.ncbi.nlm.nih.gov/pubmed/10638761
↑ Earnshaw WC. Apoptosis. A cellular poison cupboard Nature. 1999;397:387 PMID: https://www.ncbi.nlm.nih.gov/pubmed/9989401