Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase

The nature of the mitochondrial permeability transition pore (PTP) is still under debate. Here, through genetically modified F-ATP synthase, the authors show that PTP formation can be mediated by F-ATP synthase or by adenine nucleotide translocator, suggesting the existence of distinct but related p...

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Autores principales:	Andrea Carrer, Ludovica Tommasin, Justina Šileikytė, Francesco Ciscato, Riccardo Filadi, Andrea Urbani, Michael Forte, Andrea Rasola, Ildikò Szabò, Michela Carraro, Paolo Bernardi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ff86550a121a41e6be8159ac86257c13
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spelling	oai:doaj.org-article:ff86550a121a41e6be8159ac86257c132021-12-02T19:06:43ZDefining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase10.1038/s41467-021-25161-x2041-1723https://doaj.org/article/ff86550a121a41e6be8159ac86257c132021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25161-xhttps://doaj.org/toc/2041-1723The nature of the mitochondrial permeability transition pore (PTP) is still under debate. Here, through genetically modified F-ATP synthase, the authors show that PTP formation can be mediated by F-ATP synthase or by adenine nucleotide translocator, suggesting the existence of distinct but related permeability pathways.Andrea CarrerLudovica TommasinJustina ŠileikytėFrancesco CiscatoRiccardo FiladiAndrea UrbaniMichael ForteAndrea RasolaIldikò SzabòMichela CarraroPaolo BernardiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Andrea Carrer Ludovica Tommasin Justina Šileikytė Francesco Ciscato Riccardo Filadi Andrea Urbani Michael Forte Andrea Rasola Ildikò Szabò Michela Carraro Paolo Bernardi Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase
description	The nature of the mitochondrial permeability transition pore (PTP) is still under debate. Here, through genetically modified F-ATP synthase, the authors show that PTP formation can be mediated by F-ATP synthase or by adenine nucleotide translocator, suggesting the existence of distinct but related permeability pathways.
format	article
author	Andrea Carrer Ludovica Tommasin Justina Šileikytė Francesco Ciscato Riccardo Filadi Andrea Urbani Michael Forte Andrea Rasola Ildikò Szabò Michela Carraro Paolo Bernardi
author_facet	Andrea Carrer Ludovica Tommasin Justina Šileikytė Francesco Ciscato Riccardo Filadi Andrea Urbani Michael Forte Andrea Rasola Ildikò Szabò Michela Carraro Paolo Bernardi
author_sort	Andrea Carrer
title	Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase
title_short	Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase
title_full	Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase
title_fullStr	Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase
title_full_unstemmed	Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase
title_sort	defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of f-atp synthase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ff86550a121a41e6be8159ac86257c13
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Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase

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