Further Investigation of FAS-Associating Death Doman-Like Interleukin-1𝛽-Converting Enzyme, A Homologous ICE/CED-3-Like Protease Recruited to the CD95 (FAS/APO-1) Death=Inducing Signaling Complex
Previous research has identified CAP3 and CAP4, components of the CD95 (Fas/APO-1) death-inducing signaling complex, by the use of nano-electrospray tandem mass spectrometry, a recently developed technique to sequence quantities of polyacrylamide gel-separated proteins. Interestingly, CAP4 encodes a novel 55kDa protein, designated FLICE, which has homology to both FADD and the ICE/CED-3 family of cysteine proteases. FLICE binds to the death effector domain of FADD and upon overexpression induces apoptosis that is blocked by the ICE family inhibitors, CrmA and z-V AD-fink. CAP3 was identified as the FLICE prodomain which likely remains bound to the receptor after proteolytic activation. This further investigation provides unique biochemical evidence to link a death receptor physically to the proapoptotic proteases of the ICE/CED-3 family.
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