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A coiled coil trigger site is essential for rapid binding of synaptobrevin to the SNARE acceptor complex.

MPS-Authors
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Wiederhold,  K.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Walter,  A. M.
Research Group of Molecular Mechanisms of the Exocytosis, MPI for biophysical chemistry, Max Planck Society;

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Stein,  A.
Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Kienle,  N.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Sörensen,  J. B.
Research Group of Molecular Mechanisms of the Exocytosis, MPI for biophysical chemistry, Max Planck Society;

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Fasshauer,  D.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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956646-Suppl.pdf
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Citation

Wiederhold, K., Klöpper, T. H., Walter, A. M., Stein, A., Kienle, N., Sörensen, J. B., et al. (2010). A coiled coil trigger site is essential for rapid binding of synaptobrevin to the SNARE acceptor complex. Journal of Biological Chemistry, 285(28), 21549-21559. doi:10.1074/jbc.M110.105148.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0011-F048-2
Abstract
Exocytosis from synaptic vesicles is driven by stepwise formation of a tight α-helical complex between the fusing membranes. The complex is composed of the three SNAREs: synaptobrevin 2, SNAP-25, and syntaxin 1a. An important step in complex formation is fast binding of vesicular synaptobrevin to the preformed syntaxin 1·SNAP-25 dimer. Exactly how this step relates to neurotransmitter release is not well understood. Here, we combined different approaches to gain insights into this reaction. Using computational methods, we identified a stretch in synaptobrevin 2 that may function as a coiled coil “trigger site.” This site is also present in many synaptobrevin homologs functioning in other trafficking steps. Point mutations in this stretch inhibited binding to the syntaxin 1·SNAP-25 dimer and slowed fusion of liposomes. Moreover, the point mutations severely inhibited secretion from chromaffin cells. Altogether, this demonstrates that the trigger site in synaptobrevin is crucial for productive SNARE zippering.