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. 1995 Nov 15;14(22):5579-88.
doi: 10.1002/j.1460-2075.1995.tb00245.x.

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

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

F C Kischkel et al. EMBO J. .

Abstract

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

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References

    1. J Biol Chem. 1994 Oct 28;269(43):26614-7 - PubMed
    1. Annu Rev Immunol. 1994;12:555-92 - PubMed
    1. Nature. 1995 May 4;375(6526):81-3 - PubMed
    1. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4268-72 - PubMed
    1. J Biol Chem. 1995 Jan 6;270(1):387-91 - PubMed

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