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• W2013061840 abstract "The synaptic protein interaction (synprint) site of the voltage-gated Ca(2+) channel (VGCC) alpha1 subunit can interact with proteins involved in exocytosis, and it is therefore thought to be essential for exocytosis of synaptic vesicles. Here we report that the synprint site can also directly bind the mu subunit of AP-2, an adaptor protein for clathrin-mediated endocytosis, in competition with the synaptotagmin 1 (Syt 1) C2B domain. In brain lysates, the AP-2-synprint interaction occurred over a wide range of Ca(2+) concentrations but was inhibited at high Ca(2+) concentrations, in which Syt 1 interacted with synprint site. At the calyx of Held synapse in rat brainstem slices, direct presynaptic loading of the synprint fragment peptide blocked endocytic, but not exocytic, membrane capacitance changes. We propose that the VGCC synprint site is involved in synaptic vesicle endocytosis, rather than exocytosis, in the nerve terminal, via Ca(2+)-dependent interactions with AP-2 and Syt." @default.
• W2013061840 created "2016-06-24" @default.
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• W2013061840 date "2010-01-13" @default.
• W2013061840 modified "2023-10-17" @default.
• W2013061840 title "Involvement of Ca²⁺Channel Synprint Site in Synaptic Vesicle Endocytosis" @default.
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• W2013061840 doi "https://doi.org/10.1523/jneurosci.3214-09.2010" @default.
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