Structural basis of mitochondrial tethering by mitofusin complexes

Takumi Koshiba, Scott A. Detmer, Jens T. Kaiser, Hsiuchen Chen, J. Michael McCaffery, David C. Chan

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537 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)858-862
Number of pages5
Issue number5685
Publication statusPublished - Aug 6 2004


All Science Journal Classification (ASJC) codes

  • General

Cite this

Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004). Structural basis of mitochondrial tethering by mitofusin complexes. Science, 305(5685), 858-862.