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Article
Nature Structural & Molecular Biology  12, 417 - 422 (2005)
Published online: 10 April 2005; | doi:10.1038/nsmb921

Hemifusion in SNARE-mediated membrane fusion

Yibin Xu1, 3, Fan Zhang1, 3, Zengliu Su1, James A McNew2 & Yeon-Kyun Shin1

1  Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.

2  Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251-1892, USA.

3  These authors contributed equally to this work.

Correspondence should be addressed to Yeon-Kyun Shin colishin@iastate.edu
SNAREs are essential for intracellular membrane fusion. Using EPR, we determined the structure of the transmembrane domain (TMD) of the vesicle (v)-SNARE Snc2p involved in trafficking in yeast. Structural features of the TMD were used to design a v-SNARE mutant in which about half of the TMD was deleted. Liposomes containing this mutant induced outer leaflet mixing but not inner leaflet mixing when incubated with liposomes containing target membrane (t)-SNAREs. Hemifusion was also detected with wild-type SNAREs when low protein concentrations were reconstituted. Thus, these results show that SNARE-mediated fusion can transit through a hemifusion intermediate.

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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