Structural Basis of Mitochondrial Tethering by Mitofusin Complexes
California Institute of Technology · Howard Hughes Medical Institute · +3 more institutions
Abstract
Vesicle fusion involves vesicle tethering, docking, and membrane merger. We show that mitofusin, an integral mitochondrial membrane protein, is required on adjacent mitochondria to mediate fusion, which indicates that mitofusin complexes act in trans (that is, between adjacent mitochondria). A heptad repeat region (HR2) mediates mitofusin oligomerization by assembling a dimeric, antiparallel coiled coil. The transmembrane segments are located at opposite ends of the 95 angstrom coiled coil and provide a mechanism for organelle tethering. Consistent with this proposal, truncated mitofusin, in an HR2-dependent manner, causes mitochondria to become apposed with a uniform gap. Our results suggest that HR2…
Citation impact
- FWCI
- 9.52
- Percentile
- 100%
- References
- 21
Authors
6- TKTakumi Koshiba
California Institute of Technology, Howard Hughes Medical Institute, Johns Hopkins University, Johns Hopkins Medicine, University of Baltimore
- SAScott A. Detmer
California Institute of Technology, Howard Hughes Medical Institute, Johns Hopkins University, Johns Hopkins Medicine, University of Baltimore
- JTJens T. Kaiser
California Institute of Technology, Howard Hughes Medical Institute, Johns Hopkins University, Johns Hopkins Medicine, University of Baltimore
- HCHsiuchen Chen
California Institute of Technology, Howard Hughes Medical Institute, Johns Hopkins University, Johns Hopkins Medicine, University of Baltimore
- JMJ. Michael McCaffery
California Institute of Technology, Howard Hughes Medical Institute, Johns Hopkins University, Johns Hopkins Medicine, University of Baltimore
Topics & keywords
- MFN2
- Tethering
- Coiled coil
- Biophysics
- Cell biology
- Mitochondrion
- Lipid bilayer fusion
- Heptad repeat