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Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1.

Bcl-x(L), an antiapoptotic Bcl-2 family member, is postulated to function at multiple stages in the cell death pathway. The possibility that Bcl-x(L) inhibits cell death at a late (postmitochondrial) step in the death pathway is supported by this report of a novel apoptosis inhibitor, Aven, which binds to both Bcl-x(L) and the caspase regulator, Apaf-1. Identified in a yeast two-hybrid screen, Aven is broadly expressed and is conserved in other mammalian species. Only those mutants of Bcl-x(L)that retain their antiapoptotic activity are capable of binding Aven. Aven interferes with the ability of Apaf-1 to self-associate, suggesting that Aven impairs Apaf-1-mediated activation of caspases. Consistent with this idea, Aven inhibited the proteolytic activation of caspases in a cell-free extract and suppressed apoptosis induced by Apaf-1 plus caspase-9. Thus, Aven represents a new class of cell death regulator.

Pubmed ID: 10949025

Authors

  • Chau BN
  • Cheng EH
  • Kerr DA
  • Hardwick JM

Journal

Molecular cell

Publication Data

July 31, 2000

Associated Grants

  • Agency: NCI NIH HHS, Id: CA73581
  • Agency: NINDS NIH HHS, Id: NS34175
  • Agency: NINDS NIH HHS, Id: NS37402

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Apoptotic Protease-Activating Factor 1
  • Carrier Proteins
  • Caspase 9
  • Caspases
  • Cell Line
  • Dimerization
  • Enzyme Activation
  • Humans
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Protein Binding
  • Protein Structure, Quaternary
  • Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Messenger
  • Tissue Distribution
  • Transfection
  • bcl-X Protein