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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2010-1-12
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pubmed:abstractText |
We identify the leucine-rich repeat transmembrane protein LRRTM2 as a key regulator of excitatory synapse development and function. LRRTM2 localizes to excitatory synapses in transfected hippocampal neurons, and shRNA-mediated knockdown of LRRTM2 leads to a decrease in excitatory synapses without affecting inhibitory synapses. LRRTM2 interacts with PSD-95 and regulates surface expression of AMPA receptors, and lentivirus-mediated knockdown of LRRTM2 in vivo decreases the strength of evoked excitatory synaptic currents. Structure-function studies indicate that LRRTM2 induces presynaptic differentiation via the extracellular LRR domain. We identify Neurexin1 as a receptor for LRRTM2 based on affinity chromatography. LRRTM2 binds to both Neurexin 1alpha and Neurexin 1beta, and shRNA-mediated knockdown of Neurexin1 abrogates LRRTM2-induced presynaptic differentiation. These observations indicate that an LRRTM2-Neurexin1 interaction plays a critical role in regulating excitatory synapse development.
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pubmed:grant |
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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/Dlgh4 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Nrxn1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1097-4199
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pubmed:author |
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pubmed:copyrightInfo |
2009 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
24
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
799-806
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pubmed:dateRevised |
2011-3-14
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pubmed:meshHeading |
pubmed-meshheading:20064388-Animals,
pubmed-meshheading:20064388-Cell Differentiation,
pubmed-meshheading:20064388-Excitatory Postsynaptic Potentials,
pubmed-meshheading:20064388-Gene Expression Regulation, Developmental,
pubmed-meshheading:20064388-Hippocampus,
pubmed-meshheading:20064388-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:20064388-Membrane Proteins,
pubmed-meshheading:20064388-Neural Cell Adhesion Molecules,
pubmed-meshheading:20064388-Neural Pathways,
pubmed-meshheading:20064388-Organ Culture Techniques,
pubmed-meshheading:20064388-Protein Binding,
pubmed-meshheading:20064388-Protein Structure, Tertiary,
pubmed-meshheading:20064388-RNA Interference,
pubmed-meshheading:20064388-Rats,
pubmed-meshheading:20064388-Receptors, AMPA,
pubmed-meshheading:20064388-Receptors, Cell Surface,
pubmed-meshheading:20064388-Signal Transduction,
pubmed-meshheading:20064388-Synapses,
pubmed-meshheading:20064388-Synaptic Membranes
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pubmed:year |
2009
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pubmed:articleTitle |
LRRTM2 interacts with Neurexin1 and regulates excitatory synapse formation.
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pubmed:affiliation |
Neurobiology Section, Division of Biology, University of California, San Diego, La Jolla, CA 92093, 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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