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Structural Basis of Mitochondrial Tethering by Mitofusin Complexes
Ist Teil von
Science (American Association for the Advancement of Science), 2004-08, Vol.305 (5685), p.858-862
Ort / Verlag
Washington, DC: American Association for the Advancement of Science
Erscheinungsjahr
2004
Quelle
American Association for the Advancement of Science EJournals
Beschreibungen/Notizen
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.