0 327

Cited 16 times in

Emergent Synapse Organizers: LAR-RPTPs and Their Companions

DC FieldValueLanguage
dc.contributor.author엄지원-
dc.date.accessioned2017-02-24T07:44:14Z-
dc.date.available2017-02-24T07:44:14Z-
dc.date.issued2016-
dc.identifier.issn1937-6448-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/146507-
dc.description.abstractLeukocyte common antigen-related receptor tyrosine phosphatases (LAR-RPTPs) have emerged as key players that organize various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. Recent research has highlighted the roles of LAR-RPTPs at neuronal synapses in mediating distinct synaptic adhesion pathways through interactions with a host of extracellular ligands and in governing a variety of intracellular signaling cascades through binding to various scaffolds and signaling proteins. In this chapter, we review and update current research progress on the extracellular ligands of LAR-RPTPs, regulation of their extracellular interactions by alternative splicing and heparan sulfates, and their intracellular signaling machineries. In particular, we review structural insights on complexes of LAR-RPTPs with their various ligands. These studies lend support to general molecular mechanisms underlying LAR-RPTP-mediated synaptic adhesion and signaling pathways.-
dc.description.statementOfResponsibilityrestriction-
dc.format.extent39~65-
dc.languageEnglish-
dc.publisherElsevier-
dc.relation.isPartOfINTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAnimals-
dc.subject.MESHExtracellular Space/metabolism-
dc.subject.MESHHumans-
dc.subject.MESHIntracellular Space/metabolism-
dc.subject.MESHModels, Biological-
dc.subject.MESHReceptor-Like Protein Tyrosine Phosphatases, Class 2/chemistry-
dc.subject.MESHReceptor-Like Protein Tyrosine Phosphatases, Class 2/metabolism*-
dc.subject.MESHSignal Transduction-
dc.subject.MESHSynapses/metabolism*-
dc.titleEmergent Synapse Organizers: LAR-RPTPs and Their Companions-
dc.typeArticle-
dc.publisher.locationNetherlands-
dc.contributor.collegeCollege of Medicine-
dc.contributor.departmentDept. of Physiology-
dc.contributor.googleauthorK.A. Han-
dc.contributor.googleauthorS. Jeon-
dc.contributor.googleauthorJ.W. Um-
dc.contributor.googleauthorJ. Ko-
dc.identifier.doi10.1016/bs.ircmb.2016.01.002-
dc.contributor.localIdA02340-
dc.relation.journalcodeJ02874-
dc.identifier.pmid27017006-
dc.identifier.urlhttp://www.sciencedirect.com/science/article/pii/S1937644816000034-
dc.subject.keywordLAR-
dc.subject.keywordPTPδ-
dc.subject.keywordPTPσ-
dc.subject.keywordalternative splicing-
dc.subject.keywordheparan sulfate-
dc.subject.keywordligands-
dc.subject.keywordreceptor protein tyrosine phosphatase-
dc.subject.keywordsynapse development-
dc.subject.keywordsynaptic adhesion-
dc.contributor.alternativeNameUm, Ji Won-
dc.contributor.affiliatedAuthorUm, Ji Won-
dc.citation.volume324-
dc.citation.startPage39-
dc.citation.endPage65-
dc.identifier.bibliographicCitationINTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY, Vol.324 : 39-65, 2016-
dc.date.modified2017-02-24-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Physiology (생리학교실) > 1. Journal Papers

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.