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The mitochondrial contact site and cristae organizing system (MICOS) is a conserved multi-subunit complex crucial for maintaining the characteristic architecture of mitochondria. Studies with deletion mutants identified Mic10 and Mic60 as core subunits of MICOS. Mic60 has been studied in detail; however, topogenesis and function of Mic10 are unknown. We report that targeting of Mic10 to the mitochondrial inner membrane requires a positively charged internal loop, but no cleavable presequence. Both transmembrane segments of Mic10 carry a characteristic four-glycine motif, which has been found in the ring-forming rotor subunit of F1Fo-ATP synthases. Overexpression of Mic10 profoundly alters the architecture of the inner membrane independently of other MICOS components. The four-glycine motifs are dispensable for interaction of Mic10 with other MICOS subunits but are crucial for the formation of large Mic10 oligomers. Our studies identify a unique role of Mic10 oligomers in promoting the formation of inner membrane crista junctions. Copyright © 2015 Elsevier Inc. All rights reserved.


Maria Bohnert, Ralf M Zerbes, Karen M Davies, Alexander W Mühleip, Heike Rampelt, Susanne E Horvath, Thorina Boenke, Anita Kram, Inge Perschil, Marten Veenhuis, Werner Kühlbrandt, Ida J van der Klei, Nikolaus Pfanner, Martin van der Laan. Central role of Mic10 in the mitochondrial contact site and cristae organizing system. Cell metabolism. 2015 May 5;21(5):747-55

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PMID: 25955210

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