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Detailed Analysis of the Human Mitochondrial Contact Site Complex Indicate a Hierarchy of Subunits
Zitieren Sie bitte immer diese URN: urn:nbn:de:bvb:20-opus-125347
- Mitochondrial inner membrane folds into cristae, which significantly increase its surface and are important for mitochondrial function. The stability of cristae depends on the mitochondrial contact site (MICOS) complex. In human mitochondria, the inner membrane MICOS complex interacts with the outer membrane sorting and assembly machinery (SAM) complex, to form the mitochondrial intermembrane space bridging complex (MIB). We have created knockdown cell lines of most of the MICOS and MIB components and have used them to study the importance ofMitochondrial inner membrane folds into cristae, which significantly increase its surface and are important for mitochondrial function. The stability of cristae depends on the mitochondrial contact site (MICOS) complex. In human mitochondria, the inner membrane MICOS complex interacts with the outer membrane sorting and assembly machinery (SAM) complex, to form the mitochondrial intermembrane space bridging complex (MIB). We have created knockdown cell lines of most of the MICOS and MIB components and have used them to study the importance of the individual subunits for the cristae formation and complex stability. We show that the most important subunits of the MIB complex in human mitochondria are Mic60/Mitofilin, Mic19/CHCHD3 and an outer membrane component Sam50. We provide additional proof that ApoO indeed is a subunit of the MICOS and MIB complexes and propose the name Mic23 for this protein. According to our results, Mic25/CHCHD6, Mic27/ApoOL and Mic23/ApoO appear to be periphery subunits of the MICOS complex, because their depletion does not affect cristae morphology or stability of other components.…
Autor(en): | Christine Ott, Eva Dorsch, Martin Fraunholz, Sebastian Straub, Vera Kozjak-Pavlovic |
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URN: | urn:nbn:de:bvb:20-opus-125347 |
Dokumentart: | Artikel / Aufsatz in einer Zeitschrift |
Institute der Universität: | Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften |
Sprache der Veröffentlichung: | Englisch |
Titel des übergeordneten Werkes / der Zeitschrift (Englisch): | PLoS One |
Erscheinungsjahr: | 2015 |
Band / Jahrgang: | 10 |
Heft / Ausgabe: | 3 |
Seitenangabe: | e0120213 |
Originalveröffentlichung / Quelle: | PLoS ONE 10(3): e0120213. doi:10.1371/journal.pone.0120213 |
DOI: | https://doi.org/10.1371/journal.pone.0120213 |
Allgemeine fachliche Zuordnung (DDC-Klassifikation): | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Freie Schlagwort(e): | co-immunoprecipitation; membrane potential; membrane proteins; mitochondria; mitochondrial membrane; motor proteins; outer membrane proteins; protein complexes |
Datum der Freischaltung: | 27.01.2016 |
Sammlungen: | Open-Access-Publikationsfonds / Förderzeitraum 2015 |
Lizenz (Deutsch): | CC BY: Creative-Commons-Lizenz: Namensnennung |