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A role for V‐ATPase subunits in synaptic vesicle fusion?
Author(s) -
El Far Oussama,
Seagar Michael
Publication year - 2011
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.1471-4159.2011.07234.x
Subject(s) - snap25 , synaptic vesicle , vesicle fusion , synaptobrevin , snare complex , syntaxin , microbiology and biotechnology , vesicle , biology , stx1a , lipid bilayer fusion , protein subunit , biophysics , biochemistry , membrane , gene
J. Neurochem. (2011) 117 , 603–612. Abstract SNARE ( s oluble N ‐ethylmaleimide sensitive factor a ttachment protein re ceptors)‐mediated exocytotic release of neurotransmitters is a key process in neuronal communication, controlled by a number of molecular interactions. A synaptic vesicle v‐SNARE protein (VAMP2 or synaptobrevin), in association with two plasma membrane t‐SNAREs (syntaxin 1 and SNAP25), assemble to form a protein complex that is largely accepted as the minimal membrane fusion machine. Acidification of the synaptic vesicle lumen by the large multi‐subunit vacuolar proton pump (V‐ATPase) is required for loading with neurotransmitters. Recent data demonstrate a direct interaction between the c‐subunit of the V‐ATPase and VAMP2 that appears to play a role at a late step in transmitter release. In this review, we examine evidence suggesting that the V0 membrane sector of the V‐ATPase not only participates in proton pumping, but plays a second distinct role in neurosecretion, downstream of filling and close to vesicle fusion.