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Fas-associated death domain protein (FADD) recruits and activates procaspase-8 through interactions between the death effector domains of these two proteins. Cellular FLICE-inhibitory protein (c-FLIP) was identified as a molecule with sequence homology to caspase-8. It has been postulated that c-FLIP prevents formation of the competent death-inducing signaling complex in a ligand-dependent manner, through its interaction with FADD and/or caspase-8. However, the interaction of FADD and c-FLIPs (short form) in apoptosis signaling has been controversially discussed. We show the purification and the characterization of human full-length FADD and c-FLIP S expressed in Escherichia coli. The purified FADD and c-FLIP S are shown as homogeneity, respectively, in SDS-PAGE analysis and light-scattering measurements. The folding properties of the α-helical structure of FADD and the super-secondary structure of c-FLIP S proteins were characterized by circular dichroism spectroscopy. Furthermore, we report here a series of biochemical and biophysical data for FADD-c-FLIPs binding in vitro. The binding of both FADD and c-FLIPs proteins was detected by BIAcore biosensor, fluorescence measurement, and size-exclusion column (SEC).

Full-length Fas-associated Death Domain Protein Interacts with Short Form of Cellular FLICE Inhibitory Protein