The mitochondrial permeability transition pore: A mystery solved?
The permeability transition denotes an increase of the mitochondrial inner membrane permeability to solutes with molecular masses up to about 1,500 Da. It is presumed to be mediated by opening of a channel, the permeability transition pore (PTP), whose molecular nature remains a mystery. Here I brie...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2013-05-01
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| Series: | Frontiers in Physiology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fphys.2013.00095/full |
| _version_ | 1819149740967723008 |
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| author | Paolo eBernardi Paolo eBernardi |
| author_facet | Paolo eBernardi Paolo eBernardi |
| author_sort | Paolo eBernardi |
| collection | DOAJ |
| description | The permeability transition denotes an increase of the mitochondrial inner membrane permeability to solutes with molecular masses up to about 1,500 Da. It is presumed to be mediated by opening of a channel, the permeability transition pore (PTP), whose molecular nature remains a mystery. Here I briefly review the history of the PTP, discuss existing models, and present our new results indicating that reconstituted dimers of the FOF1 ATP synthase form a channel with properties identical to those of the mitochondrial megachannel, the electrophysiological equivalent of the PTP. Open questions remain, but there is now promise that the PTP can be studied by genetic methods to solve the large number of outstanding problems. |
| first_indexed | 2024-12-22T14:06:25Z |
| format | Article |
| id | doaj.art-5508b7f5d3d646e6be34b995beda8009 |
| institution | Directory Open Access Journal |
| issn | 1664-042X |
| language | English |
| last_indexed | 2024-12-22T14:06:25Z |
| publishDate | 2013-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Physiology |
| spelling | doaj.art-5508b7f5d3d646e6be34b995beda80092022-12-21T18:23:18ZengFrontiers Media S.A.Frontiers in Physiology1664-042X2013-05-01410.3389/fphys.2013.0009551825The mitochondrial permeability transition pore: A mystery solved?Paolo eBernardi0Paolo eBernardi1University of PadovaConsiglio Nazionale delle RicercheThe permeability transition denotes an increase of the mitochondrial inner membrane permeability to solutes with molecular masses up to about 1,500 Da. It is presumed to be mediated by opening of a channel, the permeability transition pore (PTP), whose molecular nature remains a mystery. Here I briefly review the history of the PTP, discuss existing models, and present our new results indicating that reconstituted dimers of the FOF1 ATP synthase form a channel with properties identical to those of the mitochondrial megachannel, the electrophysiological equivalent of the PTP. Open questions remain, but there is now promise that the PTP can be studied by genetic methods to solve the large number of outstanding problems.http://journal.frontiersin.org/Journal/10.3389/fphys.2013.00095/fullCalciumMitochondriaMitochondrial Swellingpermeability transitionmitochondrial channelsFOF1 ATP synthase |
| spellingShingle | Paolo eBernardi Paolo eBernardi The mitochondrial permeability transition pore: A mystery solved? Frontiers in Physiology Calcium Mitochondria Mitochondrial Swelling permeability transition mitochondrial channels FOF1 ATP synthase |
| title | The mitochondrial permeability transition pore: A mystery solved? |
| title_full | The mitochondrial permeability transition pore: A mystery solved? |
| title_fullStr | The mitochondrial permeability transition pore: A mystery solved? |
| title_full_unstemmed | The mitochondrial permeability transition pore: A mystery solved? |
| title_short | The mitochondrial permeability transition pore: A mystery solved? |
| title_sort | mitochondrial permeability transition pore a mystery solved |
| topic | Calcium Mitochondria Mitochondrial Swelling permeability transition mitochondrial channels FOF1 ATP synthase |
| url | http://journal.frontiersin.org/Journal/10.3389/fphys.2013.00095/full |
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