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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6943
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pubmed:dateCreated |
2003-6-26
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pubmed:abstractText |
Synapses are specialized intercellular junctions in which cell adhesion molecules connect the presynaptic machinery for neurotransmitter release to the postsynaptic machinery for receptor signalling. Neurotransmitter release requires the presynaptic co-assembly of Ca2+ channels with the secretory apparatus, but little is known about how synaptic components are organized. Alpha-neurexins, a family of >1,000 presynaptic cell-surface proteins encoded by three genes, link the pre- and postsynaptic compartments of synapses by binding extracellularly to postsynaptic cell adhesion molecules and intracellularly to presynaptic PDZ domain proteins. Using triple-knockout mice, we show that alpha-neurexins are not required for synapse formation, but are essential for Ca2+-triggered neurotransmitter release. Neurotransmitter release is impaired because synaptic Ca2+ channel function is markedly reduced, although the number of cell-surface Ca2+ channels appears normal. These data suggest that alpha-neurexins organize presynaptic terminals by functionally coupling Ca2+ channels to the presynaptic machinery.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotransmitter Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/neurexin II,
http://linkedlifedata.com/resource/pubmed/chemical/neurexin IIIalpha,
http://linkedlifedata.com/resource/pubmed/chemical/neurexophilin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1476-4687
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
26
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pubmed:volume |
423
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
939-48
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12827191-Animals,
pubmed-meshheading:12827191-Brain Stem,
pubmed-meshheading:12827191-Calcium,
pubmed-meshheading:12827191-Calcium Channels,
pubmed-meshheading:12827191-Calcium Signaling,
pubmed-meshheading:12827191-Cell Adhesion,
pubmed-meshheading:12827191-Cell Adhesion Molecules, Neuronal,
pubmed-meshheading:12827191-Cells, Cultured,
pubmed-meshheading:12827191-Evoked Potentials,
pubmed-meshheading:12827191-Exocytosis,
pubmed-meshheading:12827191-Glycoproteins,
pubmed-meshheading:12827191-Mice,
pubmed-meshheading:12827191-Mice, Inbred C57BL,
pubmed-meshheading:12827191-Mice, Knockout,
pubmed-meshheading:12827191-Mice, Transgenic,
pubmed-meshheading:12827191-Neocortex,
pubmed-meshheading:12827191-Nerve Tissue Proteins,
pubmed-meshheading:12827191-Neuropeptides,
pubmed-meshheading:12827191-Neurotransmitter Agents,
pubmed-meshheading:12827191-Recombinant Fusion Proteins,
pubmed-meshheading:12827191-Synapses,
pubmed-meshheading:12827191-Synaptic Transmission,
pubmed-meshheading:12827191-Synaptic Vesicles
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pubmed:year |
2003
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pubmed:articleTitle |
Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis.
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pubmed:affiliation |
Center for Basic Neuroscience, Department of Molecular Genetics, Dallas, Texas 75390-9111, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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