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000843804 1001_ $$0P:(DE-HGF)0$$aKarmi, Ola$$b0
000843804 245__ $$aThe unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease
000843804 260__ $$aBerlin$$bSpringer$$c2018
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000843804 520__ $$aNEET 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
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000843804 7001_ $$0P:(DE-HGF)0$$aMarjault, Henri-Baptiste$$b1
000843804 7001_ $$0P:(DE-Juel1)167431$$aPesce, Luca$$b2$$ufzj
000843804 7001_ $$0P:(DE-Juel1)145614$$aCarloni, Paolo$$b3$$ufzj
000843804 7001_ $$0P:(DE-HGF)0$$aOnuchic, Jose’ N.$$b4
000843804 7001_ $$0P:(DE-HGF)0$$aJennings, Patricia A.$$b5
000843804 7001_ $$0P:(DE-HGF)0$$aMittler, Ron$$b6
000843804 7001_ $$0P:(DE-HGF)0$$aNechushtai, Rachel$$b7$$eCorresponding author
000843804 773__ $$0PERI:(DE-600)1464026-0$$a10.1007/s00775-018-1538-8$$n4$$p599-612$$tJournal of biological inorganic chemistry$$v23$$x1432-1327$$y2018
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