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Dual inhibition of SNARE complex formation by tomosyn ensures controlled neurotransmitter release.


ABSTRACT: Neurotransmitter release from presynaptic nerve terminals is regulated by soluble NSF attachment protein receptor (SNARE) complex-mediated synaptic vesicle fusion. Tomosyn inhibits SNARE complex formation and neurotransmitter release by sequestering syntaxin-1 through its C-terminal vesicle-associated membrane protein (VAMP)-like domain (VLD). However, in tomosyn-deficient mice, the SNARE complex formation is unexpectedly decreased. In this study, we demonstrate that the N-terminal WD-40 repeat domain of tomosyn catalyzes the oligomerization of the SNARE complex. Microinjection of the tomosyn N-terminal WD-40 repeat domain into neurons prevented stimulated acetylcholine release. Thus, tomosyn inhibits neurotransmitter release by catalyzing oligomerization of the SNARE complex through the N-terminal WD-40 repeat domain in addition to the inhibitory activity of the C-terminal VLD.

SUBMITTER: Sakisaka T 

PROVIDER: S-EPMC2568027 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

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Dual inhibition of SNARE complex formation by tomosyn ensures controlled neurotransmitter release.

Sakisaka Toshiaki T   Yamamoto Yasunori Y   Mochida Sumiko S   Nakamura Michiko M   Nishikawa Kouki K   Ishizaki Hiroyoshi H   Okamoto-Tanaka Miki M   Miyoshi Jun J   Fujiyoshi Yoshinori Y   Manabe Toshiya T   Takai Yoshimi Y  

The Journal of cell biology 20081001 2


Neurotransmitter release from presynaptic nerve terminals is regulated by soluble NSF attachment protein receptor (SNARE) complex-mediated synaptic vesicle fusion. Tomosyn inhibits SNARE complex formation and neurotransmitter release by sequestering syntaxin-1 through its C-terminal vesicle-associated membrane protein (VAMP)-like domain (VLD). However, in tomosyn-deficient mice, the SNARE complex formation is unexpectedly decreased. In this study, we demonstrate that the N-terminal WD-40 repeat  ...[more]

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