CD95 death-inducing signaling complex

Medema, J. P., Scaffidi, C., Kischkel, F. C., Shevchenko, A., Mann, M., Krammer, P. H., and Peter, M. E., 1997, FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). Embo J 16 2794-2804. 

Eramo, A., Sargiacomo, M., Ricci-Vitiani, L., Todaro, M., Stassi, G., Messina, C. G., Parolini, L, Lotti, F., Sette, G., Peschle, C. De Maria, R. CD95 death-inducing signaling complex formation and internalization occur in lipid rafts of type I and type II cells. Eur J Immunol 34 (2004) 1930 0. 

Extrinsic (death receptor) pathway of caspase activation during apoptosis involves the binding of death ligands to cell surface receptors (e.g., Fas/ CD95/Apo-l or TNF receptor), recruitment of adaptor molecules Fas-associated death domain (FADD) or TNF receptor-associated death domain (TRADD) to the cytosolic end of the receptor, and formation of the death-inducing signaling complex (DISC) at the plasma membrane. DISC recruits and activates the initiator caspases, caspase-8 or -10. 

Kischkel FC, Hellbardt S, Behrmann I, Germer M, Pawlita M, Krammer PH, Peter ME. Cytotoxicity-dependent APO-1 (Eas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EM BO J1995 14 5579-5588. 

The Fas receptor (CD95) binds the Fas ligand (FasL), a transmembrane protein part of TNF family. The interaction between Fas and FasL results in the formation of death-inducing signaling complex (DISC), which contains the FADD., caspase-8, and caspase-10. In some types of cells, processed caspase-8 directly activates other members of the caspase family and triggers the execution of apoptosis of the cell. In other types of cells (type II), the Fas-DISC triggers the release of proapoptotic factors from mitochondria and the amplified activation of caspase-8 [24]. 

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