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© The Rockefeller University Press, 0021-9525/1999//903 $5.00
The Journal of Cell Biology, Volume 144, Number 5, , 1999 903-914

Cell Damage-induced Conformational Changes of the Pro-Apoptotic Protein Bak In Vivo Precede the Onset of Apoptosis

Cancer Research Campaign Molecular and Cellular Pharmacology Group, School of Biological Sciences, University of Manchester, Manchester M13 9PT, United Kingdom

Investigation of events committing cells to death revealed that a concealed NH₂-terminal epitope of the pro-apoptotic protein Bak became exposed in vivo before apoptosis. This occurred after treatment of human Jurkat or CEM-C7A T-lymphoma cells with the mechanistically disparate agents staurosporine, etoposide or dexamethasone. The rapid, up to 10-fold increase in Bak-associated immunofluorescence was measured with epitope-specific monoclonal antibodies using flow cytometry and microscopy. In contrast, using a polyclonal antibody to Bak, immunofluorescence was detected both before and after treatment. There were no differences in Bak protein content nor in subcellular location before or after treatment. Immunofluorescence showed Bcl-x_L and Bak were largely associated with mitochondria and in untreated cells they coimmunoprecipitated in the presence of nonioinic detergent. This association was significantly decreased after cell perturbation suggesting that Bcl-x_L dissociation from Bak occurred on exposure of Bak's NH₂ terminus. Multiple forms of Bak protein were observed by two dimensional electrophoresis but these were unchanged by inducers of apoptosis. This indicated that integration of cellular damage signals did not take place directly on the Bak protein. Release of proteins, including Bcl-x_L, from Bak is suggested to be an important event in commitment to death.

Key Words: flow cytometry • etoposide • staurosporine • dexamethasone • protein–protein interactions

Abbreviations used in this paper: Cy3, indocarbocyanine; DMP, dimethylpimelimidate; FCM, flow cytometry; PFA, paraformaldehyde; zVADfmk, N-benzoylcarbonyl-Val-Ala-Asp-fluoromethylketone.

The study was funded by grants from the Cancer Research Campaign and the Biotechnology and Biological Sciences Research Council. Caroline Dive is a Lister Institute Fellow. Laurence Dubrez thanks the Ligue Nationale Contre le Cancer for a travel fellowship.

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• Crompton, M. (2000). Mitochondrial intermembrane junctional complexes and their role in cell death. J. Physiol. 529: 11-21 [Abstract] [Full Text]  
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• Schuler, M., Bossy-Wetzel, E., Goldstein, J. C., Fitzgerald, P., Green, D. R. (2000). p53 Induces Apoptosis by Caspase Activation through Mitochondrial Cytochrome c Release. J. Biol. Chem. 275: 7337-7342 [Abstract] [Full Text]  
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• Taylor, S. T., Hickman, J. A., Dive, C. (2000). Epigenetic Determinants of Resistance to Etoposide Regulation of Bcl-xL and Bax by Tumor Microenvironmental Factors. JNCI J Natl Cancer Inst 92: 18-23 [Abstract] [Full Text]  

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