| pubmed-article:18367087 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C0011570 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C1333711 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C1412186 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C1417814 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C0796679 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C0443252 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C0295885 | lld:lifeskim |
| pubmed-article:18367087 | lifeskim:mentions | umls-concept:C0723595 | lld:lifeskim |
| pubmed-article:18367087 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:18367087 | pubmed:dateCreated | 2008-3-27 | lld:pubmed |
| pubmed-article:18367087 | pubmed:abstractText | Matrix metalloproteases (MMPs) play a role in remodeling the extracellular matrix during brain development and have been implicated in synaptic plasticity. Here, we report that a member of the neuronal pentraxin (NP) family, neuronal pentraxin receptor (NPR), undergoes regulated cleavage by the MMP tumor necrosis factor-alpha converting enzyme (TACE). NPR is enriched at excitatory synapses where it associates with AMPA-type glutamate receptors (AMPAR) and enhances synaptogenesis. However, in response to activation of group 1 mGluRs (mGluR1/5), TACE cleaves NPR and releases the pentraxin domain from its N-terminal transmembrane domain. Cleaved NPR rapidly accumulates in endosomes where it colocalizes with AMPAR. This process is necessary for mGluR1/5-dependent LTD in hippocampal and cerebellar synapses. These observations suggest that cleaved NPR functions to "capture" AMPAR for endocytosis and reveal a bifunctional role of NPs in both synapse strengthening and weakening. | lld:pubmed |
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| pubmed-article:18367087 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18367087 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18367087 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18367087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18367087 | pubmed:status | MEDLINE | lld:pubmed |
