Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.

Defects in mitochondrial function activate compensatory responses in the cell. Mitochondrial stress that is caused by unfolded proteins inside the organelle induces a transcriptional response (termed the "mitochondrial unfolded protein response" [UPRmt]) that is mediated by activating tran...

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Autores principales:	Maria Sladowska, Michał Turek, Min-Ji Kim, Krzysztof Drabikowski, Ben Hur Marins Mussulini, Karthik Mohanraj, Remigiusz A Serwa, Ulrike Topf, Agnieszka Chacinska
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/1e1f62b124cb4c2ba9c4c19570b57648
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spelling	oai:doaj.org-article:1e1f62b124cb4c2ba9c4c19570b576482021-12-02T19:54:23ZProteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.1544-91731545-788510.1371/journal.pbio.3001302https://doaj.org/article/1e1f62b124cb4c2ba9c4c19570b576482021-07-01T00:00:00Zhttps://doi.org/10.1371/journal.pbio.3001302https://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Defects in mitochondrial function activate compensatory responses in the cell. Mitochondrial stress that is caused by unfolded proteins inside the organelle induces a transcriptional response (termed the "mitochondrial unfolded protein response" [UPRmt]) that is mediated by activating transcription factor associated with stress 1 (ATFS-1). The UPRmt increases mitochondrial protein quality control. Mitochondrial dysfunction frequently causes defects in the import of proteins, resulting in the accumulation of mitochondrial proteins outside the organelle. In yeast, cells respond to mistargeted mitochondrial proteins by increasing activity of the proteasome in the cytosol (termed the "unfolded protein response activated by mistargeting of proteins" [UPRam]). The presence and relevance of this response in higher eukaryotes is unclear. Here, we demonstrate that defects in mitochondrial protein import in Caenorhabditis elegans lead to proteasome activation and life span extension. Both proteasome activation and life span prolongation partially depend on ATFS-1, despite its lack of influence on proteasomal gene transcription. Importantly, life span prolongation depends on the fully assembled proteasome. Our data provide a link between mitochondrial dysfunction and proteasomal activity and demonstrate its direct relevance to mechanisms that promote longevity.Maria SladowskaMichał TurekMin-Ji KimKrzysztof DrabikowskiBen Hur Marins MussuliniKarthik MohanrajRemigiusz A SerwaUlrike TopfAgnieszka ChacinskaPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 19, Iss 7, p e3001302 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Maria Sladowska Michał Turek Min-Ji Kim Krzysztof Drabikowski Ben Hur Marins Mussulini Karthik Mohanraj Remigiusz A Serwa Ulrike Topf Agnieszka Chacinska Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.
description	Defects in mitochondrial function activate compensatory responses in the cell. Mitochondrial stress that is caused by unfolded proteins inside the organelle induces a transcriptional response (termed the "mitochondrial unfolded protein response" [UPRmt]) that is mediated by activating transcription factor associated with stress 1 (ATFS-1). The UPRmt increases mitochondrial protein quality control. Mitochondrial dysfunction frequently causes defects in the import of proteins, resulting in the accumulation of mitochondrial proteins outside the organelle. In yeast, cells respond to mistargeted mitochondrial proteins by increasing activity of the proteasome in the cytosol (termed the "unfolded protein response activated by mistargeting of proteins" [UPRam]). The presence and relevance of this response in higher eukaryotes is unclear. Here, we demonstrate that defects in mitochondrial protein import in Caenorhabditis elegans lead to proteasome activation and life span extension. Both proteasome activation and life span prolongation partially depend on ATFS-1, despite its lack of influence on proteasomal gene transcription. Importantly, life span prolongation depends on the fully assembled proteasome. Our data provide a link between mitochondrial dysfunction and proteasomal activity and demonstrate its direct relevance to mechanisms that promote longevity.
format	article
author	Maria Sladowska Michał Turek Min-Ji Kim Krzysztof Drabikowski Ben Hur Marins Mussulini Karthik Mohanraj Remigiusz A Serwa Ulrike Topf Agnieszka Chacinska
author_facet	Maria Sladowska Michał Turek Min-Ji Kim Krzysztof Drabikowski Ben Hur Marins Mussulini Karthik Mohanraj Remigiusz A Serwa Ulrike Topf Agnieszka Chacinska
author_sort	Maria Sladowska
title	Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.
title_short	Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.
title_full	Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.
title_fullStr	Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.
title_full_unstemmed	Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.
title_sort	proteasome activity contributes to pro-survival response upon mild mitochondrial stress in caenorhabditis elegans.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/1e1f62b124cb4c2ba9c4c19570b57648
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Proteasome activity contributes to pro-survival response upon mild mitochondrial stress in Caenorhabditis elegans.

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