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| Item Type: | Article |
|---|---|
| Title: | Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions |
| Creators Name: | Hessenberger, M., Zerbes, R.M., Rampelt, H., Kunz, S., Xavier, A.H., Purfürst, B., Lilie, H., Pfanner, N., van der Laan, M. and Daumke, O. |
| Abstract: | The mitochondrial contact site and cristae organizing system (MICOS) is crucial for the formation of crista junctions and mitochondrial inner membrane architecture. MICOS contains two core components. Mic10 shows membrane-bending activity, whereas Mic60 (mitofilin) forms contact sites between inner and outer membranes. Here we report that Mic60 deforms liposomes into thin membrane tubules and thus displays membrane-shaping activity. We identify a membrane-binding site in the soluble intermembrane space-exposed part of Mic60. This membrane-binding site is formed by a predicted amphipathic helix between the conserved coiled-coil and mitofilin domains. The mitofilin domain negatively regulates the membrane-shaping activity of Mic60. Binding of Mic19 to the mitofilin domain modulates this activity. Membrane binding and shaping by the conserved Mic60-Mic19 complex is crucial for crista junction formation, mitochondrial membrane architecture and efficient respiratory activity. Mic60 thus plays a dual role by shaping inner membrane crista junctions and forming contact sites with the outer membrane. |
| Keywords: | Amino Acid Sequence, Amino Acid Sequence Homology, Cell Membrane, Liposomes, Mitochondrial Membranes, Mitochondrial Proteins, Protein Binding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins |
| Source: | Nature Communications |
| ISSN: | 2041-1723 |
| Publisher: | Nature Publishing Group |
| Volume: | 8 |
| Page Range: | 15258 |
| Date: | 31 May 2017 |
| Official Publication: | https://doi.org/10.1038/ncomms15258 |
| PubMed: | View item in PubMed |
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