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Interaction of Daxx, a Fas binding protein, with sentrin and Ubc9.

Sentrin is a ubiquitin-like protein that can covalently modify cellular proteins, and is a Fas binding protein that protects cells against anti-Fas induced cell death. However, the mechanism by which sentrin exerts its effect upon Fas-mediated apoptosis is not well known. Thus, this study examined the interaction of sentrin with Daxx. Sentrin interacted with Daxx but not with FADD when analyzed by yeast two-hybrid assay. In vitro translated Daxx bound to GST-sentrin fusion protein. FLAG-sentrin fusion protein was also coimmunoprecipitated with Daxx in BOSC23 cells. Also, Daxx interacted with Ubc9, an essential protein as a key conjugating enzyme. Amino acids 625-740 of Daxx, known as Fas binding region, was also mapped as sentrin and Ubc9 binding region. Colocalization of Fas, sentrin, and Ubc9 binding regions suggests the importance of that region upon the regulation of Daxx. Our data also demonstrated that sentrin could homooligomerize by protein-protein interaction.

Pubmed ID: 11112409

Authors

  • Ryu SW
  • Chae SK
  • Kim E

Journal

Biochemical and biophysical research communications

Publication Data

December 9, 2000

Associated Grants

None

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Antigens, CD95
  • Base Sequence
  • Carrier Proteins
  • DNA Primers
  • Intracellular Signaling Peptides and Proteins
  • Ligases
  • Nuclear Proteins
  • Protein Binding
  • SUMO-1 Protein
  • Signal Transduction
  • Two-Hybrid System Techniques
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitins