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Abstract Mitochondrial homeostasis is maintained through complex regulatory mechanisms, including the balance of mitochondrial dynamics involving fusion and fission processes. A central player in this regulation is the ubiquitin–proteasome system (UPS), which controls the degradation of pivotal mitochondrial proteins. In this study, we identified cullin–RING E3 ligase 2 (CRL2) and its substrate receptor, FEM1B, as critical regulators of mitochondrial dynamics.
Highlights • The Fe-S proteome is destabilized when the synthesis of its cofactor is impaired • METTL17, a mitoribosome assembly factor, is depleted without Fe-S cluster biosynthesis • METTL17 binds a previously unrecognized [4Fe4S]2+ cluster • Overexpression of METTL17 rescues the bioenergetic defects of frataxin null cells Summary Friedreich’s ataxia (FA) is a debilitating, multisystemic disease caused by the depletion of frataxin (FXN), a mitochondrial iron-sulfur (Fe-S) cluster biogenesis...
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Achebach S. Selmer T. Unden G. Properties and significance of apoFNR as a second form of air-inactivated [4Fe-4S].FNR of Escherichia coli. FEBS J. 2005; 272: 4260-4269 Alvarez S.W. Sviderskiy V.O. Terzi E.M. Papagiannakopoulos T. Moreira A.L. Adams S. Sabatini D.M. Birsoy K. Possemato R. NFS1 undergoes positive selection in lung tumours and protects cells from ferroptosis. Nature. 2017; 551: 639-643 Andreini C. Banci L. Rosato A. Exploiting Bacterial Operons To Illuminate Human Iron-Sulfur Proteins. J.
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