MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death

Proc Natl Acad Sci U S A. 1997 Oct 14;94(21):11333-8. doi: 10.1073/pnas.94.21.11333.

Abstract

Activation of the cascade of proteolytic caspases has been identified as the final common pathway of apoptosis in diverse biological systems. We have isolated a gene, termed MRIT, that possesses overall sequence homology to FLICE (MACH), a large prodomain caspase that links the aggregated complex of the death domain receptors of the tumor necrosis factor receptor family to downstream caspases. However, unlike FLICE, the C-terminal domain of MRIT lacks the caspase catalytic consensus sequence QAC(R/Q)G. Nonetheless MRIT activates caspase-dependent death. Using yeast two-hybrid assays, we demonstrate that MRIT associates with caspases possessing large and small prodomains (FLICE, and CPP32/YAMA), as well as with the adaptor molecule FADD. In addition, MRIT simultaneously and independently interacts with BclXL and FLICE in mammalian cells. Thus, MRIT is a mammalian protein that interacts simultaneously with both caspases and a Bcl-2 family member.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adult
  • Amino Acid Sequence
  • Animals
  • Apoptosis*
  • Arabidopsis Proteins*
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Caspase 1
  • Cell Line
  • Cricetinae
  • Cysteine Endopeptidases / chemistry*
  • Cysteine Endopeptidases / metabolism*
  • Fatty Acid Desaturases / chemistry
  • Fatty Acid Desaturases / metabolism
  • Female
  • Humans
  • Intracellular Signaling Peptides and Proteins*
  • Lymphocytes / immunology
  • Lymphocytes / metabolism
  • Mammals
  • Molecular Sequence Data
  • Organ Specificity
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Pregnancy
  • Proto-Oncogene Proteins c-bcl-2 / chemistry
  • Proto-Oncogene Proteins c-bcl-2 / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Transcription, Genetic
  • Transfection
  • bcl-X Protein

Substances

  • Arabidopsis Proteins
  • BCL2L1 protein, human
  • CASP8 and FADD-Like Apoptosis Regulating Protein
  • CFLAR protein, human
  • Carrier Proteins
  • Intracellular Signaling Peptides and Proteins
  • Plant Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Recombinant Proteins
  • bcl-X Protein
  • Fatty Acid Desaturases
  • Fad7 protein, Arabidopsis
  • Cysteine Endopeptidases
  • Caspase 1

Associated data

  • GENBANK/U85059