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Apoptosis

Bax to Bak

Nature Reviews Molecular Cell Biology volume 2, page 6 (2001)Cite this article

Members of the Bcl-2 family fall into three subfamilies. On one side of the death equation are the anti-apoptotic proteins Bcl-2 and Bcl-xL; on the other side are the pro-apoptotic members, including the Bax subfamily (Bax and Bak) and the 'BH3-only' proteins (such as Bid and Bad). But how do the interactions between these various proteins control apoptosis?

Reporting in Cell, Nico Tjandra and colleagues discuss the regulation of one pro-apoptotic Bcl-2 family member, Bax. They have used NMR to solve its solution structure — a structure, say the authors, that is strikingly similar to that of Bcl-xL. Both contain nine α-helices, with the first eight (α1–α8) occupying almost identical positions despite low sequence similarity. But whereas Bcl-xL (right-hand figure) contains a hydrophobic pocket that can accommodate another protein (here, the Bak BH3 peptide; yellow), in Bax this pocket is occupied by its own α9 helix (green). How, then, does Bax interact with other members of the Bcl-2 family?

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References

ORIGINAL RESEARCH PAPERS

  1. Wei, M. C. et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev. 14, 2060–2071 (2000)

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  2. Suzuki, M., Youle, R. J. & Tjandra, N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103, 645–654 (2000)

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FURTHER READING

  1. Zha, J. et al. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 290, 1761–1765 (2000)

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Authors
  1. Alison Mitchell
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Mitchell, A. Bax to Bak. Nat Rev Mol Cell Biol 2, 6 (2001). https://doi.org/10.1038/35048038

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