The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease

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dc.citation.firstpage599en_US
dc.citation.issueNumber4en_US
dc.citation.journalTitleJournal of Biological Inorganic Chemistryen_US
dc.citation.lastpage612en_US
dc.citation.volumeNumber23en_US
dc.contributor.authorKarmi, Olaen_US
dc.contributor.authorMarjault, Henri-Baptisteen_US
dc.contributor.authorPesce, Lucaen_US
dc.contributor.authorCarloni, Paoloen_US
dc.contributor.authorOnuchic, José N.en_US
dc.contributor.authorJennings, Patricia A.en_US
dc.contributor.authorMittler, Ronen_US
dc.contributor.authorNechushtai, Rachelen_US
dc.contributor.orgCenter for Theoretical Biological Physicsen_US
dc.date.accessioned2018-07-11T18:51:12Zen_US
dc.date.available2018-07-11T18:51:12Zen_US
dc.date.issued2018en_US
dc.description.abstractNEET proteins comprise a new class of [2Fe-2S] cluster proteins. In human, three genes encode for NEET proteins: cisd1 encodes mitoNEET (mNT), cisd2 encodes the Nutrient-deprivation autophagy factor-1 (NAF-1) and cisd3 encodes MiNT (Miner2). These recently discovered proteins play key roles in many processes related to normal metabolism and disease. Indeed, NEET proteins are involved in iron, Fe-S, and reactive oxygen homeostasis in cells and play an important role in regulating apoptosis and autophagy. mNT and NAF-1 are homodimeric and reside on the outer mitochondrial membrane. NAF-1 also resides in the membranes of the ER associated mitochondrial membranes (MAM) and the ER. MiNT is a monomer with distinct asymmetry in the molecular surfaces surrounding the clusters. Unlike its paralogs mNT and NAF-1, it resides within the mitochondria. NAF-1 and mNT share similar backbone folds to the plant homodimeric NEET protein (At-NEET), while MiNT's backbone fold resembles a bacterial MiNT protein. Despite the variation of amino acid composition among these proteins, all NEET proteins retained their unique CDGSH domain harboring their unique 3Cys:1His [2Fe-2S] cluster coordination through evolution. The coordinating exposed His was shown to convey the lability to the NEET proteins' [2Fe-2S] clusters. In this minireview, we discuss the NEET fold and its structural elements. Special attention is given to the unique lability of the NEETs' [2Fe-2S] cluster and the implication of the latter to the NEET proteins' cellular and systemic function in health and disease.en_US
dc.identifier.citationKarmi, Ola, Marjault, Henri-Baptiste, Pesce, Luca, et al.. "The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease." <i>Journal of Biological Inorganic Chemistry,</i> 23, no. 4 (2018) Springer: 599-612. https://doi.org/10.1007/s00775-018-1538-8.en_US
dc.identifier.doihttps://doi.org/10.1007/s00775-018-1538-8en_US
dc.identifier.urihttps://hdl.handle.net/1911/102395en_US
dc.language.isoengen_US
dc.publisherSpringeren_US
dc.rightsThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.subject.keywordCisd(1–3) encoded NEET proteinsen_US
dc.subject.keywordIron-sulfur clustersen_US
dc.subject.keywordNEET-cluster labilityen_US
dc.subject.keywordNEET-folden_US
dc.subject.keyword[2Fe-2S]en_US
dc.titleThe unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and diseaseen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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