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

M. Meijer, P. Burkhardt, H. de Wit, R.F.G. Toonen, D. Fasshauer, M. Verhage

Research output: Contribution to JournalArticleAcademicpeer-review

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. © 2012 European Molecular Biology Organization | All Rights Reserved.
Original languageEnglish
Pages (from-to)2156-2168
JournalEMBO Journal
Volume31
Issue number9
DOIs
Publication statusPublished - 2012

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