Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore

Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore

The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. Here authors demonstrate that the membrane embedded bovine F-ATP synthase elicits Ca2 + -dependent currents matching those of the MMC/PTP.

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Autores principales: Andrea Urbani, Valentina Giorgio, Andrea Carrer, Cinzia Franchin, Giorgio Arrigoni, Chimari Jiko, Kazuhiro Abe, Shintaro Maeda, Kyoko Shinzawa-Itoh, Janna F. M. Bogers, Duncan G. G. McMillan, Christoph Gerle, Ildikò Szabò, Paolo Bernardi
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Q
Acceso en línea:https://doaj.org/article/4a5ef2a2afab45b2bd9dd7713ba29e76
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spelling oai:doaj.org-article:4a5ef2a2afab45b2bd9dd7713ba29e762021-12-02T17:02:08ZPurified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore10.1038/s41467-019-12331-12041-1723https://doaj.org/article/4a5ef2a2afab45b2bd9dd7713ba29e762019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12331-1https://doaj.org/toc/2041-1723The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. Here authors demonstrate that the membrane embedded bovine F-ATP synthase elicits Ca2 + -dependent currents matching those of the MMC/PTP.Andrea UrbaniValentina GiorgioAndrea CarrerCinzia FranchinGiorgio ArrigoniChimari JikoKazuhiro AbeShintaro MaedaKyoko Shinzawa-ItohJanna F. M. BogersDuncan G. G. McMillanChristoph GerleIldikò SzabòPaolo BernardiNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Andrea Urbani
Valentina Giorgio
Andrea Carrer
Cinzia Franchin
Giorgio Arrigoni
Chimari Jiko
Kazuhiro Abe
Shintaro Maeda
Kyoko Shinzawa-Itoh
Janna F. M. Bogers
Duncan G. G. McMillan
Christoph Gerle
Ildikò Szabò
Paolo Bernardi
Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
description The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. Here authors demonstrate that the membrane embedded bovine F-ATP synthase elicits Ca2 + -dependent currents matching those of the MMC/PTP.
format article
author Andrea Urbani
Valentina Giorgio
Andrea Carrer
Cinzia Franchin
Giorgio Arrigoni
Chimari Jiko
Kazuhiro Abe
Shintaro Maeda
Kyoko Shinzawa-Itoh
Janna F. M. Bogers
Duncan G. G. McMillan
Christoph Gerle
Ildikò Szabò
Paolo Bernardi
author_facet Andrea Urbani
Valentina Giorgio
Andrea Carrer
Cinzia Franchin
Giorgio Arrigoni
Chimari Jiko
Kazuhiro Abe
Shintaro Maeda
Kyoko Shinzawa-Itoh
Janna F. M. Bogers
Duncan G. G. McMillan
Christoph Gerle
Ildikò Szabò
Paolo Bernardi
author_sort Andrea Urbani
title Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
title_short Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
title_full Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
title_fullStr Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
title_full_unstemmed Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
title_sort purified f-atp synthase forms a ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/4a5ef2a2afab45b2bd9dd7713ba29e76
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