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Daxx, a novel Fas-binding protein that activates JNK and apoptosis.

The Fas cell surface receptor induces apoptosis upon receptor oligomerization. We have identified a novel signaling protein, termed Daxx, that binds specifically to the Fas death domain. Overexpression of Daxx enhances Fas-mediated apoptosis and activates the Jun N-terminal kinase (JNK) pathway. A C-terminal portion of Daxx interacts with the Fas death domain, while a different region activates both JNK and apoptosis. The Fas-binding domain of Daxx is a dominant-negative inhibitor of both Fas-induced apoptosis and JNK activation, while the FADD death domain partially inhibits death but not JNK activation. The Daxx apoptotic pathway is sensitive to both Bcl-2 and dominant-negative JNK pathway components and acts cooperatively with the FADD pathway. Thus, Daxx and FADD define two distinct apoptotic pathways downstream of Fas.

Pubmed ID: 9215629


  • Yang X
  • Khosravi-Far R
  • Chang HY
  • Baltimore D



Publication Data

June 27, 1997

Associated Grants

  • Agency: NCI NIH HHS, Id: CA51462
  • Agency: NCI NIH HHS, Id: R01 CA051462
  • Agency: NCI NIH HHS, Id: R01 CA051462-17

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Antigens, CD95
  • Apoptosis
  • Arabidopsis Proteins
  • Blotting, Northern
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Carrier Proteins
  • Cloning, Molecular
  • DNA, Complementary
  • Fatty Acid Desaturases
  • Gene Deletion
  • HeLa Cells
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • JNK Mitogen-Activated Protein Kinases
  • Mice
  • Mitogen-Activated Protein Kinases
  • Molecular Sequence Data
  • Mutagenesis
  • Nuclear Proteins
  • Plant Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Messenger
  • Receptors, Cell Surface
  • Signal Transduction
  • Yeasts