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Helical extension of the neuronal SNARE complex into the membrane

Author

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  • Alexander Stein

    (Department of Neurobiology,)

  • Gert Weber

    (Research Group X-ray Crystallography, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany
    Freie Universität Berlin, Fachbereich Biologie, Chemie, Pharmazie, Institut für Chemie und Biochemie, AG Strukturbiochemie, Takustraße 6, D-14195 Berlin, Germany)

  • Markus C. Wahl

    (Research Group X-ray Crystallography, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany
    Freie Universität Berlin, Fachbereich Biologie, Chemie, Pharmazie, Institut für Chemie und Biochemie, AG Strukturbiochemie, Takustraße 6, D-14195 Berlin, Germany)

  • Reinhard Jahn

    (Department of Neurobiology,)

Abstract

Neuronal SNARE complex structure Neurotransmission critically relies on synaptic vesicles fusing with the membrane of nerve cells to release their neurotransmitter content into the synaptic cleft, a process requiring the assembly of several members of the SNARE protein family. Stein et al. have now solved the X-ray crystallographic structure of an extended neuronal SNARE complex, which suggest that these proteins operate like nanomachines whose zippering all the way into the membranes triggers their fusion. Other SNAREs are likely to function as such robust and simple membrane fusion catalysts during most secretory or endocytosis events in eukaryotes.

Suggested Citation

  • Alexander Stein & Gert Weber & Markus C. Wahl & Reinhard Jahn, 2009. "Helical extension of the neuronal SNARE complex into the membrane," Nature, Nature, vol. 460(7254), pages 525-528, July.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7254:d:10.1038_nature08156
    DOI: 10.1038/nature08156
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    Cited by:

    1. Lijun Shi & Chenguang Yang & Mingyuan Zhang & Kangning Li & Keying Wang & Li Jiao & Ruming Liu & Yunyun Wang & Ming Li & Yong Wang & Lu Ma & Shuxin Hu & Xin Bian, 2024. "Dissecting the mechanism of atlastin-mediated homotypic membrane fusion at the single-molecule level," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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