Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death.

Fas/APO-1 and p55 tumor necrosis factor (TNF) receptor (p55-R) activate cellular mechanisms that result in cell death. Upon activation of these receptors, Fas/APO-1 binds a protein called MORT1 (or FADD) and p55-R binds a protein called TRADD. MORT1 and TRADD can also bind to each other. We have cloned a ...
novel protein, MACH, that binds to MORT1. This protein exists in multiple isoforms, some of which contain a region that has proteolytic activity and shows marked sequence homology to proteases of the ICE/CED-3 family. Cellular expression of the proteolytic MACH isoforms results in cell death. Expression of MACH isoforms that contain an incomplete ICE/CED-3 region provides effective protection against the cytotoxicity induced by Fas/APO-1 or p55-R triggering. These findings suggest that MACH is the most upstream enzymatic component in the Fas/APO-1- and p55-R-induced cell death signaling cascades.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Antigens, CD, Antigens, CD95, Apoptosis, Base Sequence, Caenorhabditis elegans Proteins, Carrier Proteins, Caspase 1, Caspases, Cell Line, Cloning, Molecular, Cysteine Endopeptidases, DNA-Binding Proteins, Fas-Associated Death Domain Protein, Helminth Proteins, Humans, Kidney, Molecular Sequence Data, Organ Specificity, Protein Binding, Proteins, RNA, Messenger, Receptors, Tumor Necrosis Factor, Receptors, Tumor Necrosis Factor, Type I, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Signal Transduction, TNF Receptor-Associated Factor 1
Cell
Date: Jun. 14, 1996
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