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Munc18-1 promotes larger dense-core vesicle docking

MPG-Autoren
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Voets,  T.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Moser,  T.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Rettig,  J.
Department of Membrane Biophysics, 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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Zitation

Voets, T., Toonen, R. F., Brian, E. C., de Wit, H., Moser, T., Rettig, J., et al. (2001). Munc18-1 promotes larger dense-core vesicle docking. Neuron, 31(4), 581-591. doi:10.1016/S0896-6273(01)00391-9.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0012-F762-0
Zusammenfassung
Secretory vesicles dock at the plasma membrane before Ca2+ 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.