ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

Sanchón et al find that misfolded proteins formed in the ER can become associated with mitochondria, both in mammalian cells and in yeast, resulting in impaired mitochondrial function. They further discover that components of ERMES-mediated ER-mitochondria contacts are needed for this mechanism, whi...

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Autores principales:	Adrián Cortés Sanchón, Harshitha Santhosh Kumar, Matilde Mantovani, Ivan Osinnii, José María Mateos, Andres Kaech, Dimitri Shcherbakov, Rashid Akbergenov, Erik C. Böttger
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/bf08851619654161a435709327ef2900
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spelling	oai:doaj.org-article:bf08851619654161a435709327ef29002021-12-05T12:08:09ZER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function10.1038/s42003-021-02873-w2399-3642https://doaj.org/article/bf08851619654161a435709327ef29002021-12-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02873-whttps://doaj.org/toc/2399-3642Sanchón et al find that misfolded proteins formed in the ER can become associated with mitochondria, both in mammalian cells and in yeast, resulting in impaired mitochondrial function. They further discover that components of ERMES-mediated ER-mitochondria contacts are needed for this mechanism, which they name ERAMS, for ER-associated mitochondrial sequestration.Adrián Cortés SanchónHarshitha Santhosh KumarMatilde MantovaniIvan OsinniiJosé María MateosAndres KaechDimitri ShcherbakovRashid AkbergenovErik C. BöttgerNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Adrián Cortés Sanchón Harshitha Santhosh Kumar Matilde Mantovani Ivan Osinnii José María Mateos Andres Kaech Dimitri Shcherbakov Rashid Akbergenov Erik C. Böttger ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
description	Sanchón et al find that misfolded proteins formed in the ER can become associated with mitochondria, both in mammalian cells and in yeast, resulting in impaired mitochondrial function. They further discover that components of ERMES-mediated ER-mitochondria contacts are needed for this mechanism, which they name ERAMS, for ER-associated mitochondrial sequestration.
format	article
author	Adrián Cortés Sanchón Harshitha Santhosh Kumar Matilde Mantovani Ivan Osinnii José María Mateos Andres Kaech Dimitri Shcherbakov Rashid Akbergenov Erik C. Böttger
author_facet	Adrián Cortés Sanchón Harshitha Santhosh Kumar Matilde Mantovani Ivan Osinnii José María Mateos Andres Kaech Dimitri Shcherbakov Rashid Akbergenov Erik C. Böttger
author_sort	Adrián Cortés Sanchón
title	ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
title_short	ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
title_full	ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
title_fullStr	ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
title_full_unstemmed	ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
title_sort	er-misfolded proteins become sequestered with mitochondria and impair mitochondrial function
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/bf08851619654161a435709327ef2900
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ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

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