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| Item Type: | Article |
|---|---|
| Title: | Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis |
| Creators Name: | Bauer, M.K.A. and Schubert, A. and Rocks, O. and Grimm, S. |
| Abstract: | Here, we describe the isolation of adenine nucleotide translocase-1 (ANT-1) in a screen for dominant, apoptosis-inducing genes. ANT-1 is a component of the mitochondrial permeability transition complex, a protein aggregate connecting the inner with the outer mitochondrial membrane that has recently been implicated in apoptosis. ANT-1 expression led to all features of apoptosis, such as phenotypic alterations, collapse of the mitochondrial membrane potential, cytochrome c release, caspase activation, and DNA degradation. Both point mutations that impair ANT-1 in its known activity to transport ADP and ATP as well as the NH(2)-terminal half of the protein could still induce apoptosis. Interestingly, ANT-2, a highly homologous protein could not lead to cell death, demonstrating the specificity of the signal for apoptosis induction. In contrast to Bax, a proapoptotic Bcl-2 gene, ANT-1 was unable to elicit a form of cell death in yeast. This and the observed repression of apoptosis by the ANT-1-interacting protein cyclophilin D suggest that the suicidal effect of ANT-1 is mediated by specific protein-protein interactions within the permeability transition pore. |
| Keywords: | Apoptosis, Cell Death, Cell Division, Cell Line, Cyclophilins, Immunophilins, Intracellular Membranes, Membrane Potentials, Mitochondria, ATP Translocases Mitochondrial ADP, Peptide Fragments, Permeability, Saccharomyces cerevisiae, Animals, Cricetinae, Mice |
| Source: | Journal of Cell Biology |
| ISSN: | 0021-9525 |
| Publisher: | Rockefeller University Press |
| Volume: | 147 |
| Number: | 7 |
| Page Range: | 1493-1502 |
| Date: | 27 December 1999 |
| Official Publication: | https://doi.org/10.1083/jcb.147.7.1493 |
| PubMed: | View item in PubMed |
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