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Publication : Structural basis of mitochondrial tethering by mitofusin complexes.

First Author  Koshiba T Year  2004
Journal  Science Volume  305
Issue  5685 Pages  858-62
PubMed ID  15297672 Mgi Jnum  J:92425
Mgi Id  MGI:3052606 Doi  10.1126/science.1099793
Citation  Koshiba T, et al. (2004) Structural basis of mitochondrial tethering by mitofusin complexes. Science 305(5685):858-62
abstractText  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.
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