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Molecular profiling of synaptic vesicle docking sites reveals novel proteins but few differences between glutamatergic and GABAergic synapses.

Authors: Boyken, Janina  Grønborg, Mads  Riedel, Dietmar  Urlaub, Henning  Jahn, Reinhard  Chua, John Jia En 
Citation: Boyken J, etal., Neuron. 2013 Apr 24;78(2):285-97. doi: 10.1016/j.neuron.2013.02.027.
Pubmed: (View Article at PubMed) PMID:23622064
DOI: Full-text: DOI:10.1016/j.neuron.2013.02.027

Neurotransmission involves calcium-triggered fusion of docked synaptic vesicles at specialized presynaptic release sites. While many of the participating proteins have been identified, the molecular composition of these sites has not been characterized comprehensively. Here, we report a procedure to biochemically isolate fractions highly enriched in docked synaptic vesicles. The fraction is largely free of postsynaptic proteins and most other organelles while containing most known synaptic vesicle and active zone proteins. Numerous presynaptic transmembrane proteins were also identified, together with over 30 uncharacterized proteins, many of which are evolutionarily conserved. Quantitative proteomic comparison of glutamate- and GABA-specific docking complexes revealed that, except of neurotransmitter-specific enzymes and transporters, only few proteins were selectively enriched in either fraction. We conclude that the core machinery involved in vesicle docking and exocytosis does not show compositional differences between the two types of synapses.

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CRRD Object Information
CRRD ID: 13702180
Created: 2018-07-18
Species: All species
Last Modified: 2018-07-18
Status: ACTIVE



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