| http://purl.uniprot.org/citations/20139422 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20139422 | http://www.w3.org/2000/01/rdf-schema#comment | "Synaptic cell adhesion molecules regulate various steps of synapse formation. The trans-synaptic adhesion between postsynaptic NGL-3 (for netrin-G ligand-3) and presynaptic LAR (for leukocyte antigen-related) regulates excitatory synapse formation in a bidirectional manner. However, little is known about the molecular details of the NGL-3-LAR adhesion and whether two additional LAR family proteins, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma, also interact with NGL-3 and are involved in synapse formation. We report here that the leucine-rich repeat (LRR) domain of NGL-3, containing nine LRRs, interacts with the first two fibronectin III (FNIII) domains of LAR to induce bidirectional synapse formation. Moreover, Gln-96 in the first LRR motif of NGL-3 is critical for LAR binding and induction of presynaptic differentiation. PTPdelta and PTPsigma also interact with NGL-3 via their first two FNIII domains. These two interactions promote synapse formation in a different manner; the PTPsigma-NGL-3 interaction promotes synapse formation in a bidirectional manner, whereas the PTPdelta-NGL-3 interaction instructs only presynaptic differentiation in a unidirectional manner. mRNAs encoding LAR family proteins display overlapping and differential expression patterns in various brain regions. These results suggest that trans-synaptic adhesion between NGL-3 and the three LAR family proteins regulates excitatory synapse formation in shared and distinct neural circuits."xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109.061127"xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/author | "Kim E."xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/author | "Kim H."xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/author | "Kim S.Y."xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/author | "Kwon S.K."xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/author | "Woo J."xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/pages | "13966-13978"xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/title | "Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation."xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://purl.uniprot.org/core/volume | "285"xsd:string |
| http://purl.uniprot.org/citations/20139422 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20139422 |
| http://purl.uniprot.org/citations/20139422 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20139422 |
| http://purl.uniprot.org/uniprot/Q64605#attribution-C53BFC9B724D9CB5D085F9FA05AFE70C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/20139422 |
| http://purl.uniprot.org/uniprot/Q64604#attribution-C53BFC9B724D9CB5D085F9FA05AFE70C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/20139422 |
| http://purl.uniprot.org/uniprot/A6KQY2#attribution-C53BFC9B724D9CB5D085F9FA05AFE70C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/20139422 |
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