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The Functions of Munc18‐1 in Regulated Exocytosis
Author(s) -
Burgoyne Robert D.,
Barclay Jeff W.,
Ciufo Leo F.,
Graham Margaret E.,
Handley Mark T.W.,
Morgan Alan
Publication year - 2009
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2008.03987.x
Subject(s) - exocytosis , munc 18 , microbiology and biotechnology , syntaxin , lipid bilayer fusion , snare complex , chemistry , stx1a , vesicle fusion , secretory vesicle , vesicle , cytosol , synaptic vesicle , biology , secretion , biochemistry , membrane , enzyme
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 1 and the other SNARE proteins and influences all of the steps leading to exocytosis, including vesicle recruitment, tethering, docking, priming, and membrane fusion.