期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 429, 期 8, 页码 1162-1170出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2017.03.006
关键词
mitochondria; MICOS; membrane architecture; inner membrane; cell organelles
资金
- Deutsche Forschungsgemeinschaft [PF 202/8-1]
- Excellence Initiative of the German federal and state governments [EXC 294 BIOSS]
- Excellence Initiative of the German federal and state governments (GSC-4 Spemann Graduate School)
- Peter and Traudl Engelhorn Stiftung
- German Academy of Sciences Leopoldina [LPDS 2013-08]
- [Sonderforschungsbereich 746]
The mitochondria! contact site and cristae organizing system (MICOS) is crucial for maintaining the architecture of the mitochondrial inner membrane. MICOS is enriched at crista junctions that connect the two inner membrane domains: inner boundary membrane and cristae membrane. MICOS promotes the formation of crista junctions, whereas the oligomeric F1F0-ATP synthase is crucial for shaping cristae rims, indicating antagonistic functions of these machineries in organizing inner membrane architecture. We report that the MICOS core subunit Mic10, but not Mic60, binds to the F1F0-ATP synthase. Mic10 selectively associates with the dimeric form of the ATP synthase and supports the formation of ATP synthase oligomers. Our results suggest that Mic10 plays a dual role in mitochondrial inner membrane architecture. In addition to its central function in sculpting crista junctions, a fraction of Mic10 molecules interact with the cristae rim-forming F1F0-ATP synthase. (C) 2017 Elsevier Ltd. All rights reserved.
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