| Literature DB >> 11545717 |
T Voets1, R F Toonen, E C Brian, H de Wit, T Moser, J Rettig, T C Südhof, E Neher, M Verhage.
Abstract
Secretory vesicles dock at the plasma membrane before Ca(2+) triggers their exocytosis. Exocytosis requires the assembly of SNARE complexes formed by the vesicle protein Synaptobrevin and the membrane proteins Syntaxin-1 and SNAP-25. We analyzed the role of Munc18-1, a cytosolic binding partner of Syntaxin-1, in large dense-core vesicle (LDCV) secretion. Calcium-dependent LDCV exocytosis was reduced 10-fold in mouse chromaffin cells lacking Munc18-1, but the kinetic properties of the remaining release, including single fusion events, were not different from controls. Concomitantly, mutant cells displayed a 10-fold reduction in morphologically docked LDCVs. Moreover, acute overexpression of Munc18-1 in bovine chromaffin cells increased the amount of releasable vesicles and accelerated vesicle supply. We conclude that Munc18-1 functions upstream of SNARE complex formation and promotes LDCV docking.Entities:
Mesh：
Substances：
Year: 2001 PMID： 11545717 DOI： 10.1016/s0896-6273(01)00391-9
Source DB: PubMed Journal: Neuron ISSN： 0896-6273 Impact factor: 17.173