Assembly of the Mitochondrial Cristae Organizer Mic10 is Regulated by Mic26-Mic27 Antagonism and CardiolipinRampelt, H., Wollweber, F., Gerke, C., de Boer, R., van der Klei, I. J., Bohnert, M., Pfanner, N. & van der Laan, M., 22-Jun-2018, In : Journal of Molecular Biology. 430, 13, p. 1883-1890 8 p.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||8|
|Journal||Journal of Molecular Biology|
|Early online date||4-May-2018|
|Publication status||Published - 22-Jun-2018|
- mitochondria, membrane architecture, protein biogenesis, protein assembly, CONTACT SITE, INNER MEMBRANE, MICOS COMPLEX, MITOFILIN COMPLEXES, PROTEIN BIOGENESIS, OUTER-MEMBRANE, SYSTEM, ARCHITECTURE, JUNCTIONS, MORPHOLOGY