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 mitochondrial 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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.jmb.2018.04.037 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Assembly of the Mitochondrial Cristae Organizer Mic10 Is Regulated by Mic26-Mic27 Antagonism and Cardiolipin.
J Mol Biol
June 2018
Medical Biochemistry and Molecular Biology, Center for Molecular Signaling, PZMS, Saarland University, 66421 Homburg, Germany.
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.
View Article and Find Full Text PDFMic10, a Core Subunit of the Mitochondrial Contact Site and Cristae Organizing System, Interacts with the Dimeric FF-ATP Synthase.
J Mol Biol
April 2017
Medical Biochemistry and Molecular Biology, Center for Molecular Signaling, PZMS, Saarland University, 66421 Homburg, Germany.
The mitochondrial 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 FF-ATP synthase is crucial for shaping cristae rims, indicating antagonistic functions of these machineries in organizing inner membrane architecture.
View Article and Find Full Text PDFDistinct Roles of Mic12 and Mic27 in the Mitochondrial Contact Site and Cristae Organizing System.
J Mol Biol
April 2016
Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104 Freiburg, Germany.
The mitochondrial inner membrane consists of two morphologically distinct domains, the inner boundary membrane and large invaginations termed cristae. Narrow membrane structures, the crista junctions, link these two domains. Maintenance of this elaborate architecture depends on the evolutionarily conserved mitochondrial contact site and cristae organizing system (MICOS), a multisubunit inner membrane protein complex.
View Article and Find Full Text PDFCentral role of Mic10 in the mitochondrial contact site and cristae organizing system.
Cell Metab
May 2015
Institut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, 79104 Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, Universität Freiburg, 79104 Freiburg, Germany. Electronic address:
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.
View Article and Find Full Text PDFMic10 Oligomerization Pinches off Mitochondrial Cristae.
Cell Metab
May 2015
Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, 50931 Cologne, Germany. Electronic address:
The mitochondrial contact site and cristae organizing system (MICOS) complex is essential for normal mitochondria biogenesis and morphology. In this issue, Bohnert et al. (2015) and Barbot et al.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!