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Palmitoylation of the synaptic vesicle fusion machinery
Author(s) -
Prescott Gerald R.,
Gorleku Oforiwa A.,
Greaves Jennifer,
Chamberlain Luke H.
Publication year - 2009
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2009.06205.x
Subject(s) - snap25 , palmitoylation , synaptotagmin 1 , vesicle fusion , stx1a , synaptic vesicle , kiss and run fusion , microbiology and biotechnology , syntaxin , snare complex , lipid bilayer fusion , biology , syntaxin 3 , munc 18 , chemistry , exocytosis , vesicle , biochemistry , secretion , membrane , cysteine , enzyme
The fusion of synaptic vesicles with the pre‐synaptic plasma membrane mediates the secretion of neurotransmitters at nerve terminals. This pathway is regulated by an array of protein–protein interactions. Of central importance are the soluble NSF ( N ‐ethylmaleimide‐sensitive factor) attachment protein receptor (SNARE) proteins syntaxin 1 and SNAP25, which are associated with the pre‐synaptic plasma membrane and vesicle‐associated membrane protein (VAMP2), a synaptic vesicle SNARE. Syntaxin 1, SNAP25 and VAMP2 interact to form a tight complex bridging the vesicle and plasma membranes, which has been suggested to represent the minimal membrane fusion machinery. Synaptic vesicle fusion is stimulated by a rise in intraterminal Ca 2+ levels, and a major Ca 2+ sensor for vesicle fusion is synaptotagmin I. Synaptotagmin is likely to couple Ca 2+ entry to vesicle fusion via Ca 2+ ‐dependent and independent interactions with membrane phospholipids and the SNARE proteins. Intriguingly, syntaxin 1, SNAP25, VAMP2 and synaptotagmin I have all been reported to be modified by palmitoylation in neurons. In this review, we discuss the mechanisms and dynamics of palmitoylation of these proteins and speculate on how palmitoylation might contribute to the regulation of synaptic vesicle fusion.