Yama/CPP32beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase

Article Abstract:

Cloning ced-3/ICE-related gene designated as Yama, which is identical to the cDNA encoding CPP32beta, revealed that Yama in purified form is a zymogen that, when activated, cleaves poly(ADP-ribose) polymerase (PARP) to generate an 85 kDa fragment observed during apoptosis. This fragment is susceptible to inhibition by CrmA, an inhibitor of interleukin-1beta (1L-1beta)-coverting enzyme. Cleavage of PARP by Yama was inhibited by CrmA but not by point mutants of CrmA, suggesting that CrmA stops cell death by inhibiting Yama.

Protease inhibitors, Proteases

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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

Article Abstract:

Molecular cloning identified a novel interacting protein, designated FADD, which binds to mutants of Fas, a receptor inducing apoptosis or programmed cell death. Point mutation of FADD has been shown to eliminate its ability to bind Fas, thereby inhibiting apoptosis. Overexpression of FADD in breast carcinoma cells induced cell death, but was suppressed by crmA, an inhibitor of the interleukin-1beta-converting enzyme. These results suggest that FADD plays a key role in the Fas signal transduction pathway.

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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex

Article Abstract:

The 55 kDa protein, designated FLICE, was encoded in the CAP4 which is an integral part of the CD95 (Fas/APO-1) cell death signaling complex. FLICE was found to bind to the FADD and ICE/CED-3 family of cysteine proteases, wherein binding of FLICE to FADD initiates cell death signaling. The binding of FLICE to ICE family of inhibitors, CrmA and z-VAD-fmk, was induced by the overexpression of FLICE-FADD which acts as a switch to close the death signal.

Proteins

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