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Journal Article

alpha-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery.

MPS-Authors
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Park,  Y.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Vennekate,  W.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

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Yavuz,  H.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Preobraschenski,  J.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Hernandez,  J. M.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Walla,  P. J.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Park, Y., Vennekate, W., Yavuz, H., Preobraschenski, J., Hernandez, J. M., Riedel, D., et al. (2014). alpha-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery. Journal of Biological Chemistry, 289(23), 16326-16335. doi:10.1074/jbc.M114.556803.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-F94D-2
Abstract
Neuronal exocytosis is mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins. Before fusion, SNARE proteins form complexes bridging the membrane followed by assembly toward the C-terminal membrane anchors, thus initiating membrane fusion. After fusion, the SNARE complex is disassembled by the AAA-ATPase N-ethylmaleimide-sensitive factor that requires the cofactor alpha-SNAP to first bind to the assembled SNARE complex. Using chromaffin granules and liposomes we now show that alpha-SNAP on its own interferes with the zippering of membrane-anchored SNARE complexes midway through the zippering reaction, arresting SNAREs in a partially assembled trans-complex and preventing fusion. Intriguingly, the interference does not result in an inhibitory effect on synaptic vesicles, suggesting that membrane properties also influence the final outcome of alpha-SNAP interference with SNARE zippering. We suggest that binding of alpha-SNAP to the SNARE complex affects the ability of the SNARE complex to harness energy or transmit force to the membrane.