Journal
MECHANISMS OF EXOCYTOSIS
Volume 1152, Issue -, Pages 76-86Publisher
BLACKWELL PUBLISHING
DOI: 10.1111/j.1749-6632.2008.03987.x
Keywords
amperometry; chromaffin cells; exocytosis; Munc18; neurotransmission; SM proteins; SNARE proteins; syntaxin
Categories
Funding
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council
- Medical Research Council
- BBSRC [BB/E006477/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E006477/1] Funding Source: researchfish
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The activation of regulated exocytosis occurs by a rise in cytosolic Ca(2+) concentration. Synaptotagmins act as the Ca(2+) sensors, whereas the machinery that allows fusion of secretory vesicles with the plasma membrane consists of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, including syntaxin 1, SNAP-25, and VAMP Within the pathway leading to exocytosis, there is an essential requirement for a member of the conserved Sec1/Munc18 (SM) protein family, which in neurotransmitter and neurohormone release in mammalian cells is Munc18-1. The exact role of Munc18-1 and the steps within exocytosis in which it acts have been intensively investigated. Current evidence suggests that Munc18-1 acts via distinct modes of interactions with syntaxin I and the other SNARE proteins and influences all of the steps leading to exocytosis, including vesicle recruitment, tethering, docking, priming, and membrane fusion.
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