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Membrane fusion

SNARE the rod, coil the complex

Nature volume 395, pages 328–329 (1998)Cite this article

Despite the continuous flux of proteins and lipids within a eukaryotic cell, its membrane-bound compartments maintain distinct identities. Their composition is regulated by the transport of cellular cargo from one organelle to another within membrane-bound vesicles — a region of the donor membrane is pinched off, then it fuses with the target membrane and delivers the cargo. This process is governed by a highly conserved machinery that includes proteins on both the vesicle and target membranes, known respectively as v- and t-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors). Sutton et al.1 (on page 347 of this issue) and Poirier et al.2 (in Nature Structural Biology) now take a step towards understanding the function of SNARE complexes, by determining the structure of the regions that are important in forming the core fusion complexes.

The cytoplasmic portions of SNARE proteins contain several α-helical regions, with heptad (seven-amino-acid) repeats in their sequences. The first and fourth residues of each repeat are hydrophobic amino acids, so one face of the α-helix is hydrophobic. When the four helices of the core fusion complex interact, these faces pack against one another to produce the hydrophobic core of a coiled coil. The core fusion complex contains three proteins. A neuronal v-SNARE called synaptobrevin (also known as VAMP) and a neuronal t-SNARE known as syntaxin each contribute a single parallel helix to the structure3,4. Another neuronal t-SNARE, SNAP-25 (synaptosome-associated protein of relative molecular mass 25,000), contributes two helices, but the orientation of these helices was not known.

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Figure 1: Models of SNARE function.

References

  1. Sutton, R. B., Fasshauer, D., Jahn, R. & Brunger, A. T. Nature 395, 347–353 (1998).

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  2. Poirier, M. A. et al. Nature Struct. Biol. 5, 765–769 (1998).

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Authors and Affiliations

  1. the Department of Structural Biology, Stanford, 94305, California, USA

    William I. Weis

  2. Department of Molecular and Cellular Physiology,

    Richard H. Scheller

  3. Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, 94305, California, USA

    Richard H. Scheller

Authors
  1. William I. Weis
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  2. Richard H. Scheller
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Weis, W., Scheller, R. SNARE the rod, coil the complex. Nature 395, 328–329 (1998). https://doi.org/10.1038/26354

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