Methods to analyze the palmitoylated CD95 high molecular weight death-inducing signaling complex.
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.
Feig
Christine
C
The Ben May Department for Cancer Research, University of Chicago, Chicago, Illinois, USA.
Peter
Marcus E
ME
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D015153:Blotting, Western; D053418:Death Domain Receptor Signaling Adaptor Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D047468:Immunoprecipitation; D054878:Lipoylation; D008970:Molecular Weight; D014461:Ultracentrifugation; D019014:fas Receptor / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*
D053418:Death Domain Receptor Signaling Adaptor Proteins; D019014:fas Receptor