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Journal Article

Distinct kinetic changes in neurotransmitter release after SNARE protein cleavage

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Sakaba,  T.
Research Group of Biophysics of Synaptic Transmission, 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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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Neher,  E.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Sakaba, T., Stein, A., Jahn, R., & Neher, E. (2005). Distinct kinetic changes in neurotransmitter release after SNARE protein cleavage. Science, 309(5733), 491-494. doi:10.1126/science.1112645.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-E88D-9
Abstract
Neurotransmitter release is triggered by calcium ions and depends critically on the correct function of three types of SNARE [soluble N-ethylmaleimide–sensitive factor attachment protein (SNAP) receptor] proteins. With use of the large calyx of Held presynaptic terminal from rats, we found that cleavage of different SNARE proteins by clostridial neurotoxins caused distinct kinetic changes in neurotransmitter release. When elevating calcium ion concentration directly at the presynaptic terminal with the use of caged calcium, cleavage of SNAP-25 by botulinum toxin A (BoNT/A) produced a strong reduction in the calcium sensitivity for release, whereas cleavage of syntaxin using BoNT/C1 and synaptobrevin using tetanus toxin (TeNT) produced an all-or-nothing block without changing the kinetics of remaining vesicles. When stimulating release by calcium influx through channels, a difference between BoNT/C1 and TeNT emerged, which suggests that cleavage of synaptobrevin modifies the coupling between channels and release-competent vesicles.