DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kwon, Seok-Kyu | ko |
dc.contributor.author | Woo, Jooyeon | ko |
dc.contributor.author | Kim, Soo-Young | ko |
dc.contributor.author | Kim, Hyun | ko |
dc.contributor.author | Kim, Eunjoon | ko |
dc.date.accessioned | 2013-03-09T22:03:49Z | - |
dc.date.available | 2013-03-09T22:03:49Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2010-04 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.285, no.18, pp.13966 - 13978 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/97590 | - |
dc.description.abstract | 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 (PTP delta), and PTP sigma, 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. PTP delta and PTP sigma also interact with NGL-3 via their first two FNIII domains. These two interactions promote synapse formation in a different manner; the PTP sigma-NGL-3 interaction promotes synapse formation in a bidirectional manner, whereas the PTP delta-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. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | LEUCINE-RICH REPEAT | - |
dc.subject | HIPPOCAMPAL CHOLINERGIC INNERVATION | - |
dc.subject | CENTRAL-NERVOUS-SYSTEM | - |
dc.subject | LIPRIN-ALPHA | - |
dc.subject | MICE LACKING | - |
dc.subject | SYNAPTOGENIC PROTEINS | - |
dc.subject | SULFATE PROTEOGLYCAN | - |
dc.subject | DEFICIENT MICE | - |
dc.subject | ACTIVE ZONE | - |
dc.subject | RPTP-DELTA | - |
dc.title | Trans-synaptic Adhesions between Netrin-G Ligand-3 (NGL-3) and Receptor Tyrosine Phosphatases LAR, Protein-tyrosine Phosphatase delta (PTP delta), and PTP sigma via Specific Domains Regulate Excitatory Synapse Formation | - |
dc.type | Article | - |
dc.identifier.wosid | 000276987700071 | - |
dc.identifier.scopusid | 2-s2.0-77951577057 | - |
dc.type.rims | ART | - |
dc.citation.volume | 285 | - |
dc.citation.issue | 18 | - |
dc.citation.beginningpage | 13966 | - |
dc.citation.endingpage | 13978 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.identifier.doi | 10.1074/jbc.M109.061127 | - |
dc.contributor.localauthor | Kim, Eunjoon | - |
dc.contributor.nonIdAuthor | Kim, Soo-Young | - |
dc.contributor.nonIdAuthor | Kim, Hyun | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | LEUCINE-RICH REPEAT | - |
dc.subject.keywordPlus | HIPPOCAMPAL CHOLINERGIC INNERVATION | - |
dc.subject.keywordPlus | CENTRAL-NERVOUS-SYSTEM | - |
dc.subject.keywordPlus | LIPRIN-ALPHA | - |
dc.subject.keywordPlus | MICE LACKING | - |
dc.subject.keywordPlus | SYNAPTOGENIC PROTEINS | - |
dc.subject.keywordPlus | SULFATE PROTEOGLYCAN | - |
dc.subject.keywordPlus | DEFICIENT MICE | - |
dc.subject.keywordPlus | ACTIVE ZONE | - |
dc.subject.keywordPlus | RPTP-DELTA | - |
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