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  Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.

Meijer, M., Burkhardt, P., de Wit, H., Toonen, R. F., Fasshauer, D., & Verhage, M. (2012). Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission. The EMBO Journal, 31(9), 2156-2168. doi:10.1038/emboj.2012.72.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-9B5C-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-08CD-6
Genre: Journal Article

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 Creators:
Meijer, M., Author
Burkhardt, P.1, Author              
de Wit, H., Author
Toonen, R. F., Author
Fasshauer, D.1, Author              
Verhage, M., Author
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1Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578596              

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 Abstract: Synaptic transmission depends critically on the Sec1p/Munc18 protein Munc18-1, but it is unclear whether Munc18-1 primarily operates as a integral part of the fusion machinery or has a more upstream role in fusion complex assembly. Here, we show that point mutations in Munc18-1 that interfere with binding to the free Syntaxin1a N-terminus and strongly impair binding to assembled SNARE complexes all support normal docking, priming and fusion of synaptic vesicles, and normal synaptic plasticity in munc18-1 null mutant neurons. These data support a prevailing role of Munc18-1 before/during SNARE-complex assembly, while its continued association to assembled SNARE complexes is dispensable for synaptic transmission.

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Language(s): eng - English
 Dates: 2012-03-232012-05-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/emboj.2012.72
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Title: The EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 31 (9) Sequence Number: - Start / End Page: 2156 - 2168 Identifier: -