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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.

Pubmed ID: 8681376


  • Boldin MP
  • Goncharov TM
  • Goltsev YV
  • Wallach D



Publication Data

June 14, 1996

Associated Grants


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