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Apoptosis

Follow the fly path

Nature Reviews Molecular Cell Biology volume 4, page 176 (2003)Cite this article

The authors in question — Arnold Levine and colleagues — started with a p53-dependent pathway that had been observed in flies but not in mammals. Drosophila p53 activates the transcription of a gene called Reaper, the product of which interacts with the inhibitor of apoptosis (IAP) protein DIAP and targets it for ubiquitin-mediated proteolysis. As DIAP's role is to inhibit caspases, its destruction frees up caspases to proceed with an apoptotic response.

So could this happen in mammals? To test this, Levine and co-workers first looked for proteins that might interact with CIAP1 — the human homologue of DIAP1. They generated stable clonal HeLa cell lines that expressed a haemagglutinin-Flag-tagged CIAP1 protein, and then co-purified CIAP1 and its partners from HeLa cell lysates using M2-agarose beads, which recognize the Flag tag. In response to etoposide-induced p53-dependent apoptosis, the authors pulled down two low-molecular-weight proteins. But these weren't CIAP1's binding partners — they were fragments of CIAP1 itself.

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References

ORIGINAL RESEARCH PAPER

  1. Jin, S. et al. CIAP1 and serine protease HTRA2 are involved in a novel p53-dependent apoptosis pathway in mammals. Genes Dev 22 January 2003 (DOI:10.1101/gad.1047003)

FURTHER READING

  1. Salvesen. G. S. & Duckett, C. S. IAP proteins: blocking the road to death's door. Nature Rev. Mol. Cell Biol. 3, 401–410 (2002)

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Authors
  1. Alison Mitchell
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Mitchell, A. Follow the fly path. Nat Rev Mol Cell Biol 4, 176 (2003). https://doi.org/10.1038/nrm1058

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