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The balancing act of NEET proteins: Iron, ROS, calcium and metabolism
dc.contributor.author | Nechushtai, Rachel | |
dc.contributor.author | Karmi, Ola | |
dc.contributor.author | Zuo, Ke | |
dc.contributor.author | Marjault, Henri-Baptiste | |
dc.contributor.author | Darash-Yahana, Merav | |
dc.contributor.author | Sohn, Yang-Sung | |
dc.contributor.author | King, Skylar D. | |
dc.contributor.author | I Zandalinas, Sara | |
dc.contributor.author | Carloni, Paolo | |
dc.contributor.author | Mittler, Ron | |
dc.date.accessioned | 2021-10-01T07:23:44Z | |
dc.date.available | 2021-10-01T07:23:44Z | |
dc.date.issued | 2020-11 | |
dc.identifier.citation | Nechushtai, R., Karmi, O., Zuo, K., Marjault, H. B., Darash-Yahana, M., Sohn, Y. S., King, S. D., Zandalinas, S. I., Carloni, P., & Mittler, R. (2020). The balancing act of NEET proteins: Iron, ROS, calcium and metabolism. Biochimica et biophysica acta. Molecular cell research, 1867(11), 118805. https://doi.org/10.1016/j.bbamcr.2020.118805 | ca_CA |
dc.identifier.issn | 0167-4889 | |
dc.identifier.uri | http://hdl.handle.net/10234/194871 | |
dc.description.abstract | NEET proteins belong to a highly conserved group of [2Fe–2S] proteins found across all kingdoms of life. Due to their unique [2Fesingle bond2S] 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. | ca_CA |
dc.format.extent | 17 p. | ca_CA |
dc.format.mimetype | application/pdf | ca_CA |
dc.language.iso | eng | ca_CA |
dc.publisher | Elsevier | ca_CA |
dc.relation.isPartOf | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2020, vol. 1867, no 11 | ca_CA |
dc.rights | Copyright © Elsevier B.V. All rights reserved. | ca_CA |
dc.rights.uri | http://rightsstatements.org/vocab/CNE/1.0/ | ca_CA |
dc.subject | calcium | ca_CA |
dc.subject | cell proliferation | ca_CA |
dc.subject | endoplasmic reticulum | ca_CA |
dc.subject | iron | ca_CA |
dc.subject | iron-sulfur proteins | ca_CA |
dc.subject | mitochondria | ca_CA |
dc.subject | protein binding | ca_CA |
dc.subject | reactive oxygen Sspecies | ca_CA |
dc.subject | NEET protein | ca_CA |
dc.title | The balancing act of NEET proteins: Iron, ROS, calcium and metabolism | ca_CA |
dc.type | info:eu-repo/semantics/article | ca_CA |
dc.identifier.doi | https://doi.org/10.1016/j.bbamcr.2020.118805 | |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/H2020/ 765048/EU/ | |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | ca_CA |
dc.relation.publisherVersion | https://www.sciencedirect.com/science/article/pii/S0167488920301634 | ca_CA |
dc.description.sponsorship | This work was supported by funding from the National Science Foundation (NSF-BSF MCB-1936590, IOS-1932639, and IOS-1353886 to RM, and BSF 2015831 to RN), the Bond Life Sciences Early Concept Grant (RM), and the University of Missouri. Hsingle bondB.M. and K.Z. were supported by the European Union's Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No. 765048. We apologize to all authors of papers not mentioned in this manuscript due to space limitations. | |
dc.type.version | info:eu-repo/semantics/submittedVersion | ca_CA |
project.funder.name | National Science Foundation | ca_CA |
project.funder.name | Bond Life Sciences Early Concept Grant | ca_CA |
project.funder.name | University of Missouri | ca_CA |
project.funder.name | European Commission | ca_CA |
oaire.awardNumber | NSF-BSF MCB-1936590 | ca_CA |
oaire.awardNumber | IOS-1932639 | ca_CA |
oaire.awardNumber | IOS-1353886 | ca_CA |
oaire.awardNumber | BSF 2015831 | ca_CA |
oaire.awardNumber | 765048 | ca_CA |
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