TY  - JOUR
A1  - Eydt, Katharina
A1  - Davies, Karen M.
A1  - Behrendt, Christina
A1  - Wittig, Ilka
A1  - Reichert, Andreas
T1  - Cristae architecture is determined by an interplay of the MICOS complex and the F1FO ATP synthase via Mic27 and Mic10
T2  - Microbial cell
N2  - The inner boundary and the cristae membrane are connected by pore-like structures termed crista junctions (CJs). The MICOS complex is required for CJ formation and enriched at CJs. Here, we address the roles of the MICOS subunits Mic27 and Mic10. We observe a positive genetic interaction between Mic27 and Mic60 and deletion of Mic27 results in impaired formation of CJs and altered cristae membrane curvature. Mic27 acts in an antagonistic manner to Mic60 as it promotes oligomerization of the F1FO-ATP synthase and partially restores CJ formation in cells lacking Mic60. Mic10 impairs oligomerization of the F1FO-ATP synthase similar to Mic60. Applying complexome profiling, we observed that deletion of Mic27 destabilizes the MICOS complex but does not impair formation of a high molecular weight Mic10 subcomplex. Moreover, this Mic10 subcomplex comigrates with the dimeric F1FO-ATP synthase in a Mic27-independent manner. Further, we observed a chemical crosslink of Mic10 to Mic27 and of Mic10 to the F1FO-ATP synthase subunit e. We corroborate the physical interaction of the MICOS complex and the F1FO-ATP synthase. We propose a model in which part of the F1FO-ATP synthase is linked to the MICOS complex via Mic10 and Mic27 and by that is regulating CJ formation.
KW  - membrane structure
KW  - bioenergetics
KW  - mitochondria
KW  - cristae
KW  - membrane protein complex
KW  - crista junction
Y1  - 2017
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/44555
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-445550
SN  - 2311-2638
N1  - ristae architecture is determined by an interplay of the MICOS complex and the F1FO ATP synthase via Mic27 and Mic10 by Eydt et al. is licensed under a Creative Commons Attribution 4.0 International License.
VL  - 4
IS  - 8
SP  - 259
EP  - 272
PB  - Shared Science Publ.
CY  - Graz
ER  -