Major work elucidating the structure and function of the CD95 death inducing signaling complex (DISC) was carried in the late 1990s. Since then the DISC has become a paradigm for multiprotein signaling complexes in the apoptosis literature. We analyzed the earliest events of DISC formation with a set of different techniques and found a surprising new characteristic of the CD95 DISC. Data revealed that CD95 is palmitoylated on cysteine 199. This lipid modification enhances receptor aggregation to the high molecular weight DISC.