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CHCHD4 (MIA40) and the mitochondrial disulfide relay system
Mitochondria are pivotal for normal cellular physiology, as they perform a crucial role in diverse cellular functions and processes, including respiration and the regulation of bioenergetic and biosynthetic pathways, as well as regulating cellular signalling and transcriptional networks. In this way...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7925007/ https://www.ncbi.nlm.nih.gov/pubmed/33599699 http://dx.doi.org/10.1042/BST20190232 |
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author | Al-Habib, Hasan Ashcroft, Margaret |
author_facet | Al-Habib, Hasan Ashcroft, Margaret |
author_sort | Al-Habib, Hasan |
collection | PubMed |
description | Mitochondria are pivotal for normal cellular physiology, as they perform a crucial role in diverse cellular functions and processes, including respiration and the regulation of bioenergetic and biosynthetic pathways, as well as regulating cellular signalling and transcriptional networks. In this way, mitochondria are central to the cell's homeostatic machinery, and as such mitochondrial dysfunction underlies the pathology of a diverse range of diseases including mitochondrial disease and cancer. Mitochondrial import pathways and targeting mechanisms provide the means to transport into mitochondria the hundreds of nuclear-encoded mitochondrial proteins that are critical for the organelle's many functions. One such import pathway is the highly evolutionarily conserved disulfide relay system (DRS) within the mitochondrial intermembrane space (IMS), whereby proteins undergo a form of oxidation-dependent protein import. A central component of the DRS is the oxidoreductase coiled-coil-helix-coiled-coil-helix (CHCH) domain-containing protein 4 (CHCHD4, also known as MIA40), the human homologue of yeast Mia40. Here, we summarise the recent advances made to our understanding of the role of CHCHD4 and the DRS in physiology and disease, with a specific focus on the emerging importance of CHCHD4 in regulating the cellular response to low oxygen (hypoxia) and metabolism in cancer. |
format | Online Article Text |
id | pubmed-7925007 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-79250072021-03-08 CHCHD4 (MIA40) and the mitochondrial disulfide relay system Al-Habib, Hasan Ashcroft, Margaret Biochem Soc Trans Review Articles Mitochondria are pivotal for normal cellular physiology, as they perform a crucial role in diverse cellular functions and processes, including respiration and the regulation of bioenergetic and biosynthetic pathways, as well as regulating cellular signalling and transcriptional networks. In this way, mitochondria are central to the cell's homeostatic machinery, and as such mitochondrial dysfunction underlies the pathology of a diverse range of diseases including mitochondrial disease and cancer. Mitochondrial import pathways and targeting mechanisms provide the means to transport into mitochondria the hundreds of nuclear-encoded mitochondrial proteins that are critical for the organelle's many functions. One such import pathway is the highly evolutionarily conserved disulfide relay system (DRS) within the mitochondrial intermembrane space (IMS), whereby proteins undergo a form of oxidation-dependent protein import. A central component of the DRS is the oxidoreductase coiled-coil-helix-coiled-coil-helix (CHCH) domain-containing protein 4 (CHCHD4, also known as MIA40), the human homologue of yeast Mia40. Here, we summarise the recent advances made to our understanding of the role of CHCHD4 and the DRS in physiology and disease, with a specific focus on the emerging importance of CHCHD4 in regulating the cellular response to low oxygen (hypoxia) and metabolism in cancer. Portland Press Ltd. 2021-02-26 2021-02-18 /pmc/articles/PMC7925007/ /pubmed/33599699 http://dx.doi.org/10.1042/BST20190232 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . Open access for this article was enabled by the participation of University of Cambridge in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with JISC. |
spellingShingle | Review Articles Al-Habib, Hasan Ashcroft, Margaret CHCHD4 (MIA40) and the mitochondrial disulfide relay system |
title | CHCHD4 (MIA40) and the mitochondrial disulfide relay system |
title_full | CHCHD4 (MIA40) and the mitochondrial disulfide relay system |
title_fullStr | CHCHD4 (MIA40) and the mitochondrial disulfide relay system |
title_full_unstemmed | CHCHD4 (MIA40) and the mitochondrial disulfide relay system |
title_short | CHCHD4 (MIA40) and the mitochondrial disulfide relay system |
title_sort | chchd4 (mia40) and the mitochondrial disulfide relay system |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7925007/ https://www.ncbi.nlm.nih.gov/pubmed/33599699 http://dx.doi.org/10.1042/BST20190232 |
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