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@ARTICLE{Karmi:843804,
      author       = {Karmi, Ola and Marjault, Henri-Baptiste and Pesce, Luca and
                      Carloni, Paolo and Onuchic, Jose’ N. and Jennings,
                      Patricia A. and Mittler, Ron and Nechushtai, Rachel},
      title        = {{T}he unique fold and lability of the [2{F}e-2{S}] clusters
                      of {NEET} proteins mediate their key functions in health and
                      disease},
      journal      = {Journal of biological inorganic chemistry},
      volume       = {23},
      number       = {4},
      issn         = {1432-1327},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {FZJ-2018-01344},
      pages        = {599-612},
      year         = {2018},
      abstract     = {NEET 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},
      cin          = {IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {571 - Connectivity and Activity (POF3-571)},
      pid          = {G:(DE-HGF)POF3-571},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29435647},
      UT           = {WOS:000435600800012},
      doi          = {10.1007/s00775-018-1538-8},
      url          = {https://juser.fz-juelich.de/record/843804},
}