The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties

The interaction of the anti-apoptotic members of the Bcl-2 family with mitochondria, through their hydrophobic C-terminus, has been proposed to play a crucial role in the execution phase of apoptosis. We report here that a substitution of the C-terminal end of pro-apoptotic bax by that of anti-apopt...

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Bibliographic Details
Published in:FEBS letters 2000-12, Vol.487 (2), p.161-165
Main Authors: Oliver, Lisa, Priault, Muriel, Tremblais, Karine, LeCabellec, Marie-Thérèse, Meflah, Khaled, Manon, Stéphen, Vallette, Francois M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Apoptosis
Apoptosis - drug effects
Apoptosis - physiology
Apoptosis - radiation effects
Bax
bcl-2-Associated X Protein
bcl-X Protein
Cell Membrane - physiology
Cytosol - physiology
DEVDase
Glioma
Humans
K562 Cells
L-Lactate Dehydrogenase - analysis
Mitochondria - physiology
Mitochondrion
Molecular Sequence Data
Peptide Hydrolases - metabolism
Proto-Oncogene Proteins - chemistry
Proto-Oncogene Proteins - metabolism
Proto-Oncogene Proteins c-bcl-2 - chemistry
Proto-Oncogene Proteins c-bcl-2 - metabolism
Rats
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - physiology
Sequence Deletion
Transfection
Tumor Cells, Cultured
Ultraviolet Rays
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Summary:The interaction of the anti-apoptotic members of the Bcl-2 family with mitochondria, through their hydrophobic C-terminus, has been proposed to play a crucial role in the execution phase of apoptosis. We report here that a substitution of the C-terminal end of pro-apoptotic bax by that of anti-apoptotic bcl-xL (baxCxL) does not modify its association with mitochondria in human and rat cells or in Saccharomyces cerevisiae. In addition, while bax sensitizes these cells to apoptotic stimuli, the construct baxCxL does not affect the apoptotic response in transfected cells. These results suggest that the C-terminus of bax plays an important role in apoptosis independently of its membrane addressing/targeting mechanism.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)02330-9