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J Biol Chem. 2014 Jun 6;289(23):16326-35. doi: 10.1074/jbc.M114.556803. Epub 2014 Apr 28.

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

Author information

1
From the Department of Neurobiology.
2
From the Department of Neurobiology, the AG Biomolecular Spectroscopy and Single-Molecule Detection, and.
3
the Facility for Electron Microscopy, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen and.
4
the AG Biomolecular Spectroscopy and Single-Molecule Detection, and the Department of Biophysical Chemistry, Institute for Physical and Theoretical Chemistry, Technical University of Braunschweig, 38106 Braunschweig, Germany.
5
From the Department of Neurobiology, rjahn@gwdg.de.

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 α-SNAP to first bind to the assembled SNARE complex. Using chromaffin granules and liposomes we now show that α-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 α-SNAP interference with SNARE zippering. We suggest that binding of α-SNAP to the SNARE complex affects the ability of the SNARE complex to harness energy or transmit force to the membrane.

KEYWORDS:

Chromaffin Cells; Fusion Protein; Neurobiology; Soluble NSF Attachment Protein Receptor (SNARE); Synapse; Vesicles

PMID:
24778182
PMCID:
PMC4047401
DOI:
10.1074/jbc.M114.556803
[Indexed for MEDLINE]
Free PMC Article

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