A mitochondrial megachannel resides in monomeric F1FO ATP synthase
The ATP synthase has been suggested to contain the mitochondrial permeability transition pore (mPTP), which has a crucial role in cell death. Here the authors show that reconstituted ATP synthase monomers form voltage-gated and Ca2+ -activated channels with the key features of mPTP.
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2019-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-13766-2 |
| _version_ | 1818991835134033920 |
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| author | Nelli Mnatsakanyan Marc C. Llaguno Youshan Yang Yangyang Yan Joachim Weber Fred J. Sigworth Elizabeth A. Jonas |
| author_facet | Nelli Mnatsakanyan Marc C. Llaguno Youshan Yang Yangyang Yan Joachim Weber Fred J. Sigworth Elizabeth A. Jonas |
| author_sort | Nelli Mnatsakanyan |
| collection | DOAJ |
| description | The ATP synthase has been suggested to contain the mitochondrial permeability transition pore (mPTP), which has a crucial role in cell death. Here the authors show that reconstituted ATP synthase monomers form voltage-gated and Ca2+ -activated channels with the key features of mPTP. |
| first_indexed | 2024-12-20T20:16:34Z |
| format | Article |
| id | doaj.art-1114e6356c4045608f3cc3526a4d63ca |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T20:16:34Z |
| publishDate | 2019-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-1114e6356c4045608f3cc3526a4d63ca2022-12-21T19:27:41ZengNature PortfolioNature Communications2041-17232019-12-0110111110.1038/s41467-019-13766-2A mitochondrial megachannel resides in monomeric F1FO ATP synthaseNelli Mnatsakanyan0Marc C. Llaguno1Youshan Yang2Yangyang Yan3Joachim Weber4Fred J. Sigworth5Elizabeth A. Jonas6Section of Endocrinology, Department of Internal Medicine, Yale UniversityCenter for Cellular and Molecular Imaging, Yale UniversityDepartment of Cellular and Molecular Physiology, Yale UniversityDepartment of Cellular and Molecular Physiology, Yale UniversityDepartment of Chemistry and Biochemistry, Texas Tech UniversityDepartment of Cellular and Molecular Physiology, Yale UniversitySection of Endocrinology, Department of Internal Medicine, Yale UniversityThe ATP synthase has been suggested to contain the mitochondrial permeability transition pore (mPTP), which has a crucial role in cell death. Here the authors show that reconstituted ATP synthase monomers form voltage-gated and Ca2+ -activated channels with the key features of mPTP.https://doi.org/10.1038/s41467-019-13766-2 |
| spellingShingle | Nelli Mnatsakanyan Marc C. Llaguno Youshan Yang Yangyang Yan Joachim Weber Fred J. Sigworth Elizabeth A. Jonas A mitochondrial megachannel resides in monomeric F1FO ATP synthase Nature Communications |
| title | A mitochondrial megachannel resides in monomeric F1FO ATP synthase |
| title_full | A mitochondrial megachannel resides in monomeric F1FO ATP synthase |
| title_fullStr | A mitochondrial megachannel resides in monomeric F1FO ATP synthase |
| title_full_unstemmed | A mitochondrial megachannel resides in monomeric F1FO ATP synthase |
| title_short | A mitochondrial megachannel resides in monomeric F1FO ATP synthase |
| title_sort | mitochondrial megachannel resides in monomeric f1fo atp synthase |
| url | https://doi.org/10.1038/s41467-019-13766-2 |
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