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Transmitter release face Ca 2+ channel clusters persist at isolated presynaptic terminals
Author(s) -
Sun Li,
Li Qi,
Khanna Rajesh,
Chan Allen W.,
Wong Fiona,
Stanley Elise F.
Publication year - 2006
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.2006.04653.x
Subject(s) - postsynaptic potential , biophysics , extracellular , synapse , chemistry , neurotransmission , neuroscience , extracellular matrix , microbiology and biotechnology , biology , biochemistry , receptor
Ca 2+ influx through N‐type Ca 2+ channels (CaV2.2) is known to be critical for transmitter release at many synapses. These channels are known to be localized to transmitter release sites, but their anchoring mechanism remains unknown. Recent studies have demonstrated that presynaptic organization is subject to interactions with the postsynaptic cell or the intervening extracellular matrix. We used a previously described high‐affinity antibody against the N‐type Ca 2+ channels, Ab571, to localize Ca 2+ channel clusters at the release face of an isolated giant calyx‐type synapse to test whether the maintenance of these clusters requires an intact extracellular matrix or contact with the postsynaptic cell. Because the number of Ca 2+ channel clusters was unchanged after extracellular matrix dispersal or nerve terminal isolation, we conclude that presynaptic transmitter release face Ca 2+ clusters can be maintained independently of extracellular influences. Our results suggest that a presynaptic molecular scaffold is responsible for the maintenance of release site Ca 2+ channel clusters.