A mitofusin-dependent docking ring complex triggers mitochondrial fusion in vitro
- Fusion of mitochondrial outer membranes is crucial for proper organelle function and involves large GTPases called mitofusins. The discrete steps that allow mitochondria to attach to one another and merge their outer membranes are unknown. By combining an in vitro mitochondrial fusion assay with electron cryo-tomography (cryo-ET), we visualize the junction between attached mitochondria isolated from Saccharomyces cerevisiae and observe complexes that mediate this attachment. We find that cycles of GTP hydrolysis induce progressive formation of a docking ring structure around extended areas of contact. Further GTP hydrolysis triggers local outer membrane fusion at the periphery of the contact region. These findings unravel key features of mitofusin-dependent fusion of outer membranes and constitute an important advance in our understanding of how mitochondria connect and merge.
Author: | Tobias Brandt, Laetitia Cavellini, Werner KühlbrandtORCiDGND, Michaël M. Cohen |
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URN: | urn:nbn:de:hebis:30:3-445294 |
DOI: | https://doi.org/10.7554/eLife.14618 |
ISSN: | 2050-084X |
Pubmed Id: | https://pubmed.ncbi.nlm.nih.gov/27253069 |
Parent Title (English): | eLife |
Publisher: | eLife Sciences Publications |
Place of publication: | Cambridge |
Document Type: | Article |
Language: | English |
Date of Publication (online): | 2017/11/09 |
Year of first Publication: | 2016 |
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
Release Date: | 2017/11/09 |
Tag: | Biophysics and structural biology; Cell biology; Cryo-em; Dynamin-related-proteins; Membrane fusion; Mitochondria; Mitochondrial dynamics; Mitofusin; Research article |
Volume: | 5 |
Issue: | e14618 |
Page Number: | 23 |
First Page: | 1 |
Last Page: | 23 |
Note: | Copyright Brandt et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. |
HeBIS-PPN: | 424951258 |
Institutes: | Angeschlossene und kooperierende Institutionen / MPI für Biophysik |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Sammlungen: | Universitätspublikationen |
Licence (German): | Creative Commons - Namensnennung 4.0 |