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Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization
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| Zeitschriftentitel: | Bioscience Reports |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | Bioscience Reports, 33, 2013, 5 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
|
| Schlagwörter: |
| author_facet |
Saxena, Nishant Katiyar, Shashank P. Liu, Ye Grover, Abhinav Gao, Ran Sundar, Durai Kaul, Sunil C. Wadhwa, Renu Saxena, Nishant Katiyar, Shashank P. Liu, Ye Grover, Abhinav Gao, Ran Sundar, Durai Kaul, Sunil C. Wadhwa, Renu |
|---|---|
| author |
Saxena, Nishant Katiyar, Shashank P. Liu, Ye Grover, Abhinav Gao, Ran Sundar, Durai Kaul, Sunil C. Wadhwa, Renu |
| spellingShingle |
Saxena, Nishant Katiyar, Shashank P. Liu, Ye Grover, Abhinav Gao, Ran Sundar, Durai Kaul, Sunil C. Wadhwa, Renu Bioscience Reports Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization Cell Biology Molecular Biology Biochemistry Biophysics |
| author_sort |
saxena, nishant |
| spelling |
Saxena, Nishant Katiyar, Shashank P. Liu, Ye Grover, Abhinav Gao, Ran Sundar, Durai Kaul, Sunil C. Wadhwa, Renu 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20130034 <jats:p>Bcl-2 family of proteins consists of both pro-apoptotic and anti-apoptotic members that control cellular apoptosis. They predominantly reside in the mitochondria and control the release of apoptotic factors from the mitochondria to the cytosol by regulating its membrane potential and opening the PT (permeability transition) pore. Here we report bioinformatics and biochemical evidence to demonstrate the interaction between Bcl-2 and Bcl-xL with a stress chaperone, mortalin. We demonstrate that such interaction results in the abrogation of mortalin-p53 interaction leading to nuclear translocation and transcriptional reactivation of p53 function that results in an induction of senescence in cancer cells.</jats:p> Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization Bioscience Reports |
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Portland Press Ltd., 2013 |
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Portland Press Ltd., 2013 |
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| title |
Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_unstemmed |
Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_full |
Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_fullStr |
Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_full_unstemmed |
Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_short |
Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_sort |
molecular interactions of bcl-2 and bcl-xl with mortalin: identification and functional characterization |
| topic |
Cell Biology Molecular Biology Biochemistry Biophysics |
| url |
http://dx.doi.org/10.1042/bsr20130034 |
| publishDate |
2013 |
| physical |
|
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<jats:p>Bcl-2 family of proteins consists of both pro-apoptotic and anti-apoptotic members that control cellular apoptosis. They predominantly reside in the mitochondria and control the release of apoptotic factors from the mitochondria to the cytosol by regulating its membrane potential and opening the PT (permeability transition) pore. Here we report bioinformatics and biochemical evidence to demonstrate the interaction between Bcl-2 and Bcl-xL with a stress chaperone, mortalin. We demonstrate that such interaction results in the abrogation of mortalin-p53 interaction leading to nuclear translocation and transcriptional reactivation of p53 function that results in an induction of senescence in cancer cells.</jats:p> |
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| author | Saxena, Nishant, Katiyar, Shashank P., Liu, Ye, Grover, Abhinav, Gao, Ran, Sundar, Durai, Kaul, Sunil C., Wadhwa, Renu |
| author_facet | Saxena, Nishant, Katiyar, Shashank P., Liu, Ye, Grover, Abhinav, Gao, Ran, Sundar, Durai, Kaul, Sunil C., Wadhwa, Renu, Saxena, Nishant, Katiyar, Shashank P., Liu, Ye, Grover, Abhinav, Gao, Ran, Sundar, Durai, Kaul, Sunil C., Wadhwa, Renu |
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| description | <jats:p>Bcl-2 family of proteins consists of both pro-apoptotic and anti-apoptotic members that control cellular apoptosis. They predominantly reside in the mitochondria and control the release of apoptotic factors from the mitochondria to the cytosol by regulating its membrane potential and opening the PT (permeability transition) pore. Here we report bioinformatics and biochemical evidence to demonstrate the interaction between Bcl-2 and Bcl-xL with a stress chaperone, mortalin. We demonstrate that such interaction results in the abrogation of mortalin-p53 interaction leading to nuclear translocation and transcriptional reactivation of p53 function that results in an induction of senescence in cancer cells.</jats:p> |
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| imprint | Portland Press Ltd., 2013 |
| imprint_str_mv | Portland Press Ltd., 2013 |
| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11 |
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| publishDate | 2013 |
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| series | Bioscience Reports |
| source_id | 49 |
| spelling | Saxena, Nishant Katiyar, Shashank P. Liu, Ye Grover, Abhinav Gao, Ran Sundar, Durai Kaul, Sunil C. Wadhwa, Renu 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20130034 <jats:p>Bcl-2 family of proteins consists of both pro-apoptotic and anti-apoptotic members that control cellular apoptosis. They predominantly reside in the mitochondria and control the release of apoptotic factors from the mitochondria to the cytosol by regulating its membrane potential and opening the PT (permeability transition) pore. Here we report bioinformatics and biochemical evidence to demonstrate the interaction between Bcl-2 and Bcl-xL with a stress chaperone, mortalin. We demonstrate that such interaction results in the abrogation of mortalin-p53 interaction leading to nuclear translocation and transcriptional reactivation of p53 function that results in an induction of senescence in cancer cells.</jats:p> Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization Bioscience Reports |
| spellingShingle | Saxena, Nishant, Katiyar, Shashank P., Liu, Ye, Grover, Abhinav, Gao, Ran, Sundar, Durai, Kaul, Sunil C., Wadhwa, Renu, Bioscience Reports, Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization, Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| title | Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_full | Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_fullStr | Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_full_unstemmed | Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_short | Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| title_sort | molecular interactions of bcl-2 and bcl-xl with mortalin: identification and functional characterization |
| title_unstemmed | Molecular interactions of Bcl-2 and Bcl-xL with mortalin: identification and functional characterization |
| topic | Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| url | http://dx.doi.org/10.1042/bsr20130034 |