Structural basis of mitochondrial tethering by mitofusin complexes
| Autor: | David C. Chan, Takumi Koshiba, Jens T. Kaiser, Scott A. Detmer, Hsiuchen Chen, J. Michael McCaffery |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Vesicle fusion Molecular Sequence Data MFN2 Biology Hybrid Cells Crystallography X-Ray Membrane Fusion Vesicle tethering Protein Structure Secondary Cell Line GTP Phosphohydrolases Mice MFN1 Animals Humans Amino Acid Sequence Coiled coil Multidisciplinary Mitochondrial membrane fusion Intracellular Membranes Mitochondria Protein Structure Tertiary Heptad repeat Biochemistry Amino Acid Substitution Mitochondrial Membrane Protein Mutation Biophysics Dimerization Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Science (New York, N.Y.). 305(5685) |
| ISSN: | 1095-9203 |
| Popis: | 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 functions as a mitochondrial tether before fusion. |
| Databáze: | OpenAIRE |
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