Journal
CELL METABOLISM
Volume 21, Issue 5, Pages 747-755Publisher
CELL PRESS
DOI: 10.1016/j.cmet.2015.04.007
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Funding
- Deutsche Forschungsgemeinschaft [PF 202/8-1]
- Sonderforschungsbereich [746]
- Excellence Initiative of the German federal governments [EXC 115 CEF, EXC 294 BIOSS]
- Excellence Initiative of the German federal state [EXC 115 CEF, EXC 294 BIOSS]
- Max Planck Society
- Peter and Traudl Engelhorn Stiftung
- German Academy of Sciences Leopoldina [LPDS 2013-08]
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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 sub-units 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.
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