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시냅스뇌질환연구단
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Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion

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dc.contributor.authorJi Won Um-
dc.contributor.authorKee Hun Kim-
dc.contributor.authorBeom Seok Park-
dc.contributor.authorYeonsoo Choi-
dc.contributor.authorDoyoun Kim-
dc.contributor.authorCha Yeon Kim-
dc.contributor.authorSoo Jin Kim-
dc.contributor.authorMinhye Kim-
dc.contributor.authorJi Seung Ko-
dc.contributor.authorSeong-Gyu Lee-
dc.contributor.authorGayoung Choii-
dc.contributor.authorJungyong Nam-
dc.contributor.authorWon Do Heo-
dc.contributor.authorEun Joon Kim-
dc.contributor.authorJie-Oh Lee-
dc.contributor.authorJaewon Ko-
dc.contributor.authorHo Min Kim-
dc.date.available2015-04-19T10:57:10Z-
dc.date.created2015-01-28-
dc.date.issued2014-11-
dc.identifier.issn2041-1723-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/758-
dc.description.abstractSynaptic adhesion molecules orchestrate synaptogenesis. The presynaptic leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) regulate synapse development by interacting with postsynaptic Slit- and Trk-like family proteins (Slitrks), which harbour two extracellular leucine-rich repeats (LRR1 and LRR2). Here we identify the minimal regions of the LAR-RPTPs and Slitrks, LAR-RPTPs Ig1–3 and Slitrks LRR1, for their interaction and synaptogenic function. Subsequent crystallographic and structureguided functional analyses reveal that the splicing inserts in LAR-RPTPs are key molecular determinants for Slitrk binding and synapse formation. Moreover, structural comparison of the two Slitrk1 LRRs reveal that unique properties on the concave surface of Slitrk1 LRR1 render its specific binding to LAR-RPTPs. Finally, we demonstrate that lateral interactions between adjacent trans-synaptic LAR-RPTPs/Slitrks complexes observed in crystal lattices are critical for Slitrk1-induced lateral assembly and synaptogenic activity. Thus, we propose a model in which Slitrks mediate synaptogenic functions through direct binding to LAR-RPTPs and the subsequent lateral assembly of LAR-RPTPs/Slitrks complexes.-
dc.description.uri1-
dc.formattext/plain-
dc.language영어-
dc.publisherNATURE PUBLISHING GROUP-
dc.titleStructural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000345625000003-
dc.identifier.scopusid2-s2.0-84922637272-
dc.identifier.rimsid17151ko
dc.date.tcdate2018-10-01-
dc.contributor.affiliatedAuthorYeonsoo Choi-
dc.contributor.affiliatedAuthorDoyoun Kim-
dc.contributor.affiliatedAuthorJungyong Nam-
dc.contributor.affiliatedAuthorWon Do Heo-
dc.contributor.affiliatedAuthorEun Joon Kim-
dc.identifier.doi10.1038/ncomms6423-
dc.identifier.bibliographicCitationNATURE COMMUNICATIONS, v.5, pp.5423-
dc.citation.titleNATURE COMMUNICATIONS-
dc.citation.volume5-
dc.citation.startPage5423-
dc.date.scptcdate2018-10-01-
dc.description.wostc33-
dc.description.scptc35-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordPlusPROTEIN-TYROSINE-PHOSPHATASES-
dc.subject.keywordPlusCELL-ADHESION-
dc.subject.keywordPlusPTP-SIGMA-
dc.subject.keywordPlusTRANSSYNAPTIC INTERACTION-
dc.subject.keywordPlusEXCITATORY SYNAPSES-
dc.subject.keywordPlusNEUREXIN-
dc.subject.keywordPlusDELTA-
dc.subject.keywordPlusMOLECULES-
dc.subject.keywordPlusIMMUNOGLOBULIN-
dc.subject.keywordPlusARCHITECTURE-
Appears in Collections:
Center for Synaptic Brain Dysfunctions(시냅스 뇌질환 연구단) > 1. Journal Papers (저널논문)
Center for Cognition and Sociality(인지 및 사회성 연구단) > 1. Journal Papers (저널논문)
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