Abstract:
:Neurotransmitter release is initiated by influx of Ca2+ through voltage-gated Ca2+ channels, within 200 microseconds of the action potential arriving at the synaptic terminal, as the Ca2+ concentration increases from 100 nM to > 200 microM. Exocytosis requires high Ca2+ concentration, with a threshold of 20-50 microM and half-maximal activation at 190 microM. The synaptic membrane proteins syntaxin, 25K synaptosome-associated protein (SNAP25), and vesicle-associated membrane protein (VAMP)/synaptobrevin, are thought to form a synaptic core complex which mediates vesicle docking and membrane fusion. Synaptotagmin may be the low-affinity Ca(2+)-sensor, but other Ca(2+)-sensors are involved as residual neurotransmission persists in synaptotagmin-null mutants. Syntaxin binds to N-type Ca2+ channels at a site in the intracellular loop connecting domains II and III. Here we describe Ca(2+)-dependent interaction of this site with syntaxin and SNAP25 which has a biphasic dependence on Ca2+, with maximal binding at 20 microM free Ca2+, near the threshold for transmitter release. Ca(2+)-dependent interaction of Ca2+ channels with the synaptic core complex may be important for Ca(2+)-dependent docking and fusion of synaptic vesicles.
journal_name
Naturejournal_title
Natureauthors
Sheng ZH,Rettig J,Cook T,Catterall WAdoi
10.1038/379451a0subject
Has Abstractpub_date
1996-02-01 00:00:00pages
451-4issue
6564eissn
0028-0836issn
1476-4687journal_volume
379pub_type
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