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SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development.

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dc.contributor.author엄지원-
dc.date.accessioned2017-02-27T07:34:04Z-
dc.date.available2017-02-27T07:34:04Z-
dc.date.issued2016-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/146915-
dc.description.abstractSynaptogenic adhesion molecules play critical roles in synapse formation. SALM5/Lrfn5, a SALM/Lrfn family adhesion molecule implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons, but its presynaptic ligand remains unknown. We found that SALM5 interacts with the Ig domains of LAR family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPδ, and PTPσ). These interactions are strongly inhibited by the splice insert B in the Ig domain region of LAR-RPTPs, and mediate SALM5-dependent presynaptic differentiation in contacting axons. In addition, SALM5 regulates AMPA receptor-mediated synaptic transmission through mechanisms involving the interaction of postsynaptic SALM5 with presynaptic LAR-RPTPs. These results suggest that postsynaptic SALM5 promotes synapse development by trans-synaptically interacting with presynaptic LAR-RPTPs and is important for the regulation of excitatory synaptic strength.-
dc.description.statementOfResponsibilityopen-
dc.formatapplication/pdf-
dc.languageEnglish-
dc.publisherNature Publishing Group-
dc.relation.isPartOfSCIENTIFIC REPORTS-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAlternative Splicing/physiology*-
dc.subject.MESHAnimals-
dc.subject.MESHAxons/metabolism*-
dc.subject.MESHCell Adhesion Molecules, Neuronal/genetics-
dc.subject.MESHCell Adhesion Molecules, Neuronal/metabolism*-
dc.subject.MESHMice-
dc.subject.MESHReceptor-Like Protein Tyrosine Phosphatases, Class 2/genetics-
dc.subject.MESHReceptor-Like Protein Tyrosine Phosphatases, Class 2/metabolism*-
dc.subject.MESHSynapses/genetics-
dc.subject.MESHSynapses/metabolism*-
dc.subject.MESHSynaptic Transmission/physiology*-
dc.titleSALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development.-
dc.typeArticle-
dc.publisher.locationEngland-
dc.contributor.collegeCollege of Medicine-
dc.contributor.departmentDept. of Physiology-
dc.contributor.googleauthorYeonsoo Choi-
dc.contributor.googleauthorJungyong Nam-
dc.contributor.googleauthorDaniel J. Whitcomb-
dc.contributor.googleauthorYoo Sung Song-
dc.contributor.googleauthorDoyoun Kim-
dc.contributor.googleauthorSangmin Jeon-
dc.contributor.googleauthorJi Won Um-
dc.contributor.googleauthorSeong-Gyu Lee-
dc.contributor.googleauthorJooyeon Woo-
dc.contributor.googleauthorSeok-Kyu Kwon-
dc.contributor.googleauthorYan Li-
dc.contributor.googleauthorWon Mah-
dc.contributor.googleauthorHo Min Kim-
dc.contributor.googleauthorJaewon Ko-
dc.contributor.googleauthorKwangwook Cho-
dc.contributor.googleauthorEunjoon Kim-
dc.identifier.doi10.1038/srep26676-
dc.contributor.localIdA02340-
dc.relation.journalcodeJ02646-
dc.identifier.eissn2045-2322-
dc.identifier.pmid27225731-
dc.contributor.alternativeNameUm, Ji Won-
dc.contributor.affiliatedAuthorUm, Ji Won-
dc.citation.volume6-
dc.citation.startPage26676-
dc.identifier.bibliographicCitationSCIENTIFIC REPORTS, Vol.6 : 26676, 2016-
dc.date.modified2017-02-24-
dc.identifier.rimsid46481-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Physiology (생리학교실) > 1. Journal Papers

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