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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2011-5-10
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pubmed:databankReference |
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pubmed:abstractText |
Neurexin and neuroligin, which undergo heterophilic interactions with each other at the synapse, are mutated in some patients with autism spectrum disorder, a set of disorders characterized by deficits in social and emotional learning. We have explored the role of neurexin and neuroligin at sensory-to-motor neuron synapses of the gill-withdrawal reflex in Aplysia, which undergoes sensitization, a simple form of learned fear. We find that depleting neurexin in the presynaptic sensory neuron or neuroligin in the postsynaptic motor neuron abolishes both long-term facilitation and the associated presynaptic growth induced by repeated pulses of serotonin. Moreover, introduction into the motor neuron of the R451C mutation of neuroligin-3 linked to autism spectrum disorder blocks both intermediate-term and long-term facilitation. Our results suggest that activity-dependent regulation of the neurexin-neuroligin interaction may govern transsynaptic signaling required for the storage of long-term memory, including emotional memory that may be impaired in autism spectrum disorder.
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pubmed:grant |
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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/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/neurexin 1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/neuroligin 3
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1097-4199
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
468-81
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pubmed:dateRevised |
2011-11-14
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pubmed:meshHeading |
pubmed-meshheading:21555073-Analysis of Variance,
pubmed-meshheading:21555073-Animals,
pubmed-meshheading:21555073-Aplysia,
pubmed-meshheading:21555073-Arginine,
pubmed-meshheading:21555073-Cell Adhesion Molecules, Neuronal,
pubmed-meshheading:21555073-Cells, Cultured,
pubmed-meshheading:21555073-Central Nervous System,
pubmed-meshheading:21555073-Cloning, Molecular,
pubmed-meshheading:21555073-Cysteine,
pubmed-meshheading:21555073-Excitatory Postsynaptic Potentials,
pubmed-meshheading:21555073-Gene Expression Regulation,
pubmed-meshheading:21555073-Green Fluorescent Proteins,
pubmed-meshheading:21555073-Humans,
pubmed-meshheading:21555073-Long-Term Potentiation,
pubmed-meshheading:21555073-Membrane Proteins,
pubmed-meshheading:21555073-Microinjections,
pubmed-meshheading:21555073-Molecular Sequence Data,
pubmed-meshheading:21555073-Motor Neurons,
pubmed-meshheading:21555073-Mutation,
pubmed-meshheading:21555073-Nerve Tissue Proteins,
pubmed-meshheading:21555073-Oligodeoxyribonucleotides, Antisense,
pubmed-meshheading:21555073-Protein Binding,
pubmed-meshheading:21555073-Receptors, Cell Surface,
pubmed-meshheading:21555073-Sensory Receptor Cells,
pubmed-meshheading:21555073-Serotonin,
pubmed-meshheading:21555073-Synapses
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pubmed:year |
2011
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pubmed:articleTitle |
Neurexin-neuroligin transsynaptic interaction mediates learning-related synaptic remodeling and long-term facilitation in aplysia.
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pubmed:affiliation |
Department of Neurology, College of Physicians and Surgeons of Columbia University, New York State Psychiatric Institute, New York, NY 10032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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