Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor.

摘要: APO-1 (Fas/CD95), a member of the tumor necrosis factor receptor superfamily, induces apoptosis upon oligomerization. In search to identify intracellular signaling molecules coupling oligomerized APO-1, several cytotoxicity-dependent APO-1-associated proteins (CAP) were immunoprecipitated from apoptosis-sensitive human leukemic T cell line HUT78 and lymphoblastoid B SKW6.4. CAP1-3 (27-29 kDa) CAP4 (55 kDa), instantly detectable after crosslinking associated only with aggregated (the form APO-1) not monomeric APO-1. CAP1 CAP2 identified as serine phosphorylated MORT1/FADD. The association CAP1-4 was observed C-terminally truncated non-signaling addition, did associate an cytoplasmic tail carrying lprcg amino acid replacement. Moreover, no APO-1-CAP found in APO-1+, anti-APO-1-resistant pre-B Boe. Our data suggest that vivo are apoptosis-transducing molecules.