| pubmed-article:15540461 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15540461 | lifeskim:mentions | umls-concept:C1512777 | lld:lifeskim |
| pubmed-article:15540461 | lifeskim:mentions | umls-concept:C0386529 | lld:lifeskim |
| pubmed-article:15540461 | lifeskim:mentions | umls-concept:C0392752 | lld:lifeskim |
| pubmed-article:15540461 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:15540461 | pubmed:dateCreated | 2004-11-15 | lld:pubmed |
| pubmed-article:15540461 | pubmed:abstractText | Neuroligins are cell adhesion proteins that are thought to instruct the formation and alignment of synaptic specializations. The three known rodent neuroligin isoforms share homologous extracellular acetylcholinesterase-like domains that bridge the synaptic cleft and bind beta-neurexins. All neuroligins have identical intracellular C-terminal motifs that bind to PDZ domains of various target proteins. Neuroligin 1 is specifically localized to glutamatergic postsynaptic specializations. We show here that neuroligin 2 is exclusively localized to inhibitory synapses in rat brain and dissociated neurons. In immature neurons, neuroligin 2 is found at synapses and also at GABAA receptor aggregates that are not facing presynaptic termini, indicating that postsynaptic mechanisms lead to synaptic recruitment of neuroligin 2. Our findings identify neuroligin 2 as a new cell adhesion protein specific for inhibitory synapses and open new avenues for identifiying the constituents of this unique type of postsynaptic specialization. | lld:pubmed |
| pubmed-article:15540461 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15540461 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15540461 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15540461 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15540461 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15540461 | pubmed:issn | 0171-9335 | lld:pubmed |
| pubmed-article:15540461 | pubmed:author | pubmed-author:BroseNilsN | lld:pubmed |
| pubmed-article:15540461 | pubmed:author | pubmed-author:JamainStéphan... | lld:pubmed |
| pubmed-article:15540461 | pubmed:author | pubmed-author:VaroqueauxFré... | lld:pubmed |
| pubmed-article:15540461 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15540461 | pubmed:volume | 83 | lld:pubmed |
| pubmed-article:15540461 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15540461 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15540461 | pubmed:pagination | 449-56 | lld:pubmed |
| pubmed-article:15540461 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:15540461 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15540461 | pubmed:articleTitle | Neuroligin 2 is exclusively localized to inhibitory synapses. | lld:pubmed |
| pubmed-article:15540461 | pubmed:affiliation | Max-Planck-Institute for Experimental Medicine, Department of Molecular Neurobiology, Göttingen, Germany. | lld:pubmed |
| pubmed-article:15540461 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15540461 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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