Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 430, Issue 13, Pages 1883-1890Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2018.04.037
Keywords
mitochondria; membrane architecture; protein biogenesis; protein assembly
Categories
Funding
- Deutsche Forschungsgemeinschaft [PF 202/8-1]
- Sonderforschungsbereiche [746, 894]
- International Research Training Group 1830
- Excellence Initiative of the German federal and state governments [EXC 294 BIOSS]
- Excellence Initiative of the German federal and state governments (Spemann Graduate School) [GSC-4]
- Peter and Traudl Engelhorn Stiftung
- Boehringer Ingelhelm Fonds
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The multi-subunit mitochondrial contact site and cristae organizing system (MICOS) is a conserved protein complex of the inner mitochondrial membrane that is essential for maintenance of cristae architecture. The core subunit Mic10 forms large oligomers that build a scaffold and induce membrane curvature. The regulation of Mic10 oligomerization is poorly understood. We report that Mic26 exerts a destabilizing effect on Mic10 oligomers and thus functions in an antagonistic manner to the stabilizing subunit Mic27. The mitochondria! signature phospholipid cardiolipin shows a stabilizing function on Mic10 oligomers. Our findings indicate that the Mic10 core machinery of MICOS is regulated by several mechanisms, including interaction with cardiolipin and antagonistic actions of Mic26 and Mic27. (C) 2018 Elsevier Ltd. All rights reserved.
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