Serveur d'exploration sur les mitochondries dans l'oxydoréduction chez les plantes

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The balancing act of NEET proteins: Iron, ROS, calcium and metabolism.

Identifieur interne : 000008 ( Main/Exploration ); précédent : 000007; suivant : 000009

The balancing act of NEET proteins: Iron, ROS, calcium and metabolism.

Auteurs : Rachel Nechushtai [Israël] ; Ola Karmi [Israël] ; Ke Zuo [Allemagne] ; Henri-Baptiste Marjault [Allemagne] ; Merav Darash-Yahana [Israël] ; Yang-Sung Sohn [Israël] ; Skylar D. King [États-Unis] ; Sara I. Zandalinas [États-Unis] ; Paolo Carloni [Allemagne] ; Ron Mittler [États-Unis]

Source :

RBID : pubmed:32745723

Abstract

NEET proteins belong to a highly conserved group of [2Fe-2S] proteins found across all kingdoms of life. Due to their unique [2Fe2S] cluster structure, they play a key role in the regulation of many different redox and oxidation processes. In eukaryotes, NEET proteins are localized to the mitochondria, endoplasmic reticulum (ER) and the mitochondrial-associated membranes connecting these organelles (MAM), and are involved in the control of multiple processes, ranging from autophagy and apoptosis to ferroptosis, oxidative stress, cell proliferation, redox control and iron and iron‑sulfur homeostasis. Through their different functions and interactions with key proteins such as VDAC and Bcl-2, NEET proteins coordinate different mitochondrial, MAM, ER and cytosolic processes and functions and regulate major signaling molecules such as calcium and reactive oxygen species. Owing to their central role in cells, NEET proteins are associated with numerous human maladies including cancer, metabolic diseases, diabetes, obesity, and neurodegenerative diseases. In recent years, a new and exciting role for NEET proteins was uncovered, i.e., the regulation of mitochondrial dynamics and morphology. This new role places NEET proteins at the forefront of studies into cancer and different metabolic diseases, both associated with the regulation of mitochondrial dynamics. Here we review recent studies focused on the evolution, biological role, and structure of NEET proteins, as well as discuss different studies conducted on NEET proteins function using transgenic organisms. We further discuss the different strategies used in the development of drugs that target NEET proteins, and link these with the different roles of NEET proteins in cells.

DOI: 10.1016/j.bbamcr.2020.118805
PubMed: 32745723


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<div type="abstract" xml:lang="en">NEET proteins belong to a highly conserved group of [2Fe-2S] proteins found across all kingdoms of life. Due to their unique [2Fe2S] cluster structure, they play a key role in the regulation of many different redox and oxidation processes. In eukaryotes, NEET proteins are localized to the mitochondria, endoplasmic reticulum (ER) and the mitochondrial-associated membranes connecting these organelles (MAM), and are involved in the control of multiple processes, ranging from autophagy and apoptosis to ferroptosis, oxidative stress, cell proliferation, redox control and iron and iron‑sulfur homeostasis. Through their different functions and interactions with key proteins such as VDAC and Bcl-2, NEET proteins coordinate different mitochondrial, MAM, ER and cytosolic processes and functions and regulate major signaling molecules such as calcium and reactive oxygen species. Owing to their central role in cells, NEET proteins are associated with numerous human maladies including cancer, metabolic diseases, diabetes, obesity, and neurodegenerative diseases. In recent years, a new and exciting role for NEET proteins was uncovered, i.e., the regulation of mitochondrial dynamics and morphology. This new role places NEET proteins at the forefront of studies into cancer and different metabolic diseases, both associated with the regulation of mitochondrial dynamics. Here we review recent studies focused on the evolution, biological role, and structure of NEET proteins, as well as discuss different studies conducted on NEET proteins function using transgenic organisms. We further discuss the different strategies used in the development of drugs that target NEET proteins, and link these with the different roles of NEET proteins in cells.</div>
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<AbstractText>NEET proteins belong to a highly conserved group of [2Fe-2S] proteins found across all kingdoms of life. Due to their unique [2Fe2S] cluster structure, they play a key role in the regulation of many different redox and oxidation processes. In eukaryotes, NEET proteins are localized to the mitochondria, endoplasmic reticulum (ER) and the mitochondrial-associated membranes connecting these organelles (MAM), and are involved in the control of multiple processes, ranging from autophagy and apoptosis to ferroptosis, oxidative stress, cell proliferation, redox control and iron and iron‑sulfur homeostasis. Through their different functions and interactions with key proteins such as VDAC and Bcl-2, NEET proteins coordinate different mitochondrial, MAM, ER and cytosolic processes and functions and regulate major signaling molecules such as calcium and reactive oxygen species. Owing to their central role in cells, NEET proteins are associated with numerous human maladies including cancer, metabolic diseases, diabetes, obesity, and neurodegenerative diseases. In recent years, a new and exciting role for NEET proteins was uncovered, i.e., the regulation of mitochondrial dynamics and morphology. This new role places NEET proteins at the forefront of studies into cancer and different metabolic diseases, both associated with the regulation of mitochondrial dynamics. Here we review recent studies focused on the evolution, biological role, and structure of NEET proteins, as well as discuss different studies conducted on NEET proteins function using transgenic organisms. We further discuss the different strategies used in the development of drugs that target NEET proteins, and link these with the different roles of NEET proteins in cells.</AbstractText>
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<Affiliation>Department of Physics, RWTH Aachen University, Aachen, Germany; Computational Biomedicine, Institute of Advanced Simulation IAS-5 and Institute of Neuroscience and Medicine INM-9, Germany; JARA Institute: Molecular Neuroscience and Imaging, Institute of Neuroscience and Medicine INM-11, Forschungszentrum Jülich GmbH, 52425 Jülich, Germany.</Affiliation>
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<AffiliationInfo>
<Affiliation>Department of Surgery, University of Missouri School of Medicine, Christopher S. Bond Life Sciences Center University of Missouri. 1201 Rollins St, Columbia, MO 65211, USA; Division of Plant Sciences, College of Agriculture Food and Natural Resources and Interdisciplinary Plant Group, Christopher S. Bond Life Sciences Center University of Missouri. 1201 Rollins St, Columbia, MO 65211, USA. Electronic address: mittlerr@missouri.edu.</Affiliation>
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<Year>2020</Year>
<Month>08</Month>
<Day>01</Day>
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<Country>Netherlands</Country>
<MedlineTA>Biochim Biophys Acta Mol Cell Res</MedlineTA>
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<CoiStatement>Declaration of competing interest The authors declare no conflict of interest.</CoiStatement>
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<Month>07</Month>
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<Month>07</Month>
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<ArticleId IdType="doi">10.1016/j.bbamcr.2020.118805</ArticleId>
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<list>
<country>
<li>Allemagne</li>
<li>Israël</li>
<li>États-Unis</li>
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<li>District de Cologne</li>
<li>Missouri (État)</li>
<li>Rhénanie-du-Nord-Westphalie</li>
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<li>Aix-la-Chapelle</li>
<li>Juliers</li>
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<name sortKey="Darash Yahana, Merav" sort="Darash Yahana, Merav" uniqKey="Darash Yahana M" first="Merav" last="Darash-Yahana">Merav Darash-Yahana</name>
<name sortKey="Karmi, Ola" sort="Karmi, Ola" uniqKey="Karmi O" first="Ola" last="Karmi">Ola Karmi</name>
<name sortKey="Sohn, Yang Sung" sort="Sohn, Yang Sung" uniqKey="Sohn Y" first="Yang-Sung" last="Sohn">Yang-Sung Sohn</name>
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<name sortKey="Carloni, Paolo" sort="Carloni, Paolo" uniqKey="Carloni P" first="Paolo" last="Carloni">Paolo Carloni</name>
<name sortKey="Marjault, Henri Baptiste" sort="Marjault, Henri Baptiste" uniqKey="Marjault H" first="Henri-Baptiste" last="Marjault">Henri-Baptiste Marjault</name>
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<country name="États-Unis">
<region name="Missouri (État)">
<name sortKey="King, Skylar D" sort="King, Skylar D" uniqKey="King S" first="Skylar D" last="King">Skylar D. King</name>
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<name sortKey="Zandalinas, Sara I" sort="Zandalinas, Sara I" uniqKey="Zandalinas S" first="Sara I" last="Zandalinas">Sara I. Zandalinas</name>
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