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X-linked IAP is a direct inhibitor of cell-death proteases

Author

Listed:
  • Quinn L. Deveraux
  • Ryosuke Takahashi
  • Guy S. Salvesen

    (The Burnham Institute, Program on Apoptosis and Cell Death Research)

  • John C. Reed

    (The Burnham Institute, Program on Apoptosis and Cell Death Research)

Abstract

The inhibitor-of-apoptosis (IAP) family of genes has an evolutionarily conserved role in regulating programmed cell death in animals ranging from insects to humans1,2,3,4,5,6. Ectopic expression of human IAP proteins can suppress cell death induced by a variety of stimuli, but the mechanism of this inhibition was previously unknown. Here we show that human X-chromosome-linked IAP directly inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. As the caspases are highly conserved throughout the animal kingdom and are the principal effectors of apoptosis7, our findings suggest how IAPs might inhibit cell death, providing evidence for a mechanism of action for these mammalian cell-death suppressors.

Suggested Citation

  • Quinn L. Deveraux & Ryosuke Takahashi & Guy S. Salvesen & John C. Reed, 1997. "X-linked IAP is a direct inhibitor of cell-death proteases," Nature, Nature, vol. 388(6639), pages 300-304, July.
  • Handle: RePEc:nat:nature:v:388:y:1997:i:6639:d:10.1038_40901
    DOI: 10.1038/40901
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    Cited by:

    1. Madison L. Doolittle & Dominik Saul & Japneet Kaur & Jennifer L. Rowsey & Stephanie J. Vos & Kevin D. Pavelko & Joshua N. Farr & David G. Monroe & Sundeep Khosla, 2023. "Multiparametric senescent cell phenotyping reveals targets of senolytic therapy in the aged murine skeleton," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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