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Structural basis of mitochondrial tethering by mitofusin complexes
Author(s): Koshiba T, Detmer SA, Kaiser JT, Chen HC, McCaffery JM, Chan DC
Source: SCIENCE    Volume: 305    Issue: 5685    Pages: 858-862    Published: AUG 6 2004  
Times Cited: 121     References: 22     
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 functions as a mitochondrial tether before fusion.
Document Type: Article
Language: English
Reprint Address: Chan, DC (reprint author), CALTECH, Div Biol, 1200 E Calif Blvd,MC114-96, Pasadena, CA 91125 USA
Addresses:
1. CALTECH, Div Biol, Pasadena, CA 91125 USA
2. CALTECH, Div Chem, Pasadena, CA 91125 USA
3. Johns Hopkins Univ, Howard Hughes Med Inst, Baltimore, MD 21218 USA
4. Johns Hopkins Univ, Dept Biol, Integrated Imaging Ctr, Baltimore, MD 21218 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: 843RT
ISSN: 0036-8075
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