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dc.contributor.authorUchigashima, Motokazu
dc.contributor.authorCheung, Amy
dc.contributor.authorFutai, Kensuke
dc.date2022-08-11T08:08:28.000
dc.date.accessioned2022-08-23T15:56:13Z
dc.date.available2022-08-23T15:56:13Z
dc.date.issued2021-10-06
dc.date.submitted2021-12-20
dc.identifier.citation<p>Uchigashima M, Cheung A, Futai K. Neuroligin-3: A Circuit-Specific Synapse Organizer That Shapes Normal Function and Autism Spectrum Disorder-Associated Dysfunction. Front Mol Neurosci. 2021 Oct 6;14:749164. doi: 10.3389/fnmol.2021.749164. PMID: 34690695; PMCID: PMC8526735. <a href="https://doi.org/10.3389/fnmol.2021.749164">Link to article on publisher's site</a></p>
dc.identifier.issn1662-5099 (Linking)
dc.identifier.doi10.3389/fnmol.2021.749164
dc.identifier.pmid34690695
dc.identifier.urihttp://hdl.handle.net/20.500.14038/29922
dc.description.abstractChemical synapses provide a vital foundation for neuron-neuron communication and overall brain function. By tethering closely apposed molecular machinery for presynaptic neurotransmitter release and postsynaptic signal transduction, circuit- and context- specific synaptic properties can drive neuronal computations for animal behavior. Trans-synaptic signaling via synaptic cell adhesion molecules (CAMs) serves as a promising mechanism to generate the molecular diversity of chemical synapses. Neuroligins (Nlgns) were discovered as postsynaptic CAMs that can bind to presynaptic CAMs like Neurexins (Nrxns) at the synaptic cleft. Among the four (Nlgn1-4) or five (Nlgn1-3, Nlgn4X, and Nlgn4Y) isoforms in rodents or humans, respectively, Nlgn3 has a heterogeneous expression and function at particular subsets of chemical synapses and strong association with non-syndromic autism spectrum disorder (ASD). Several lines of evidence have suggested that the unique expression and function of Nlgn3 protein underlie circuit-specific dysfunction characteristic of non-syndromic ASD caused by the disruption of Nlgn3 gene. Furthermore, recent studies have uncovered the molecular mechanism underlying input cell-dependent expression of Nlgn3 protein at hippocampal inhibitory synapses, in which trans-synaptic signaling of specific alternatively spliced isoforms of Nlgn3 and Nrxn plays a critical role. In this review article, we overview the molecular, anatomical, and physiological knowledge about Nlgn3, focusing on the circuit-specific function of mammalian Nlgn3 and its underlying molecular mechanism. This will provide not only new insight into specific Nlgn3-mediated trans-synaptic interactions as molecular codes for synapse specification but also a better understanding of the pathophysiological basis for non-syndromic ASD associated with functional impairment in Nlgn3 gene.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=34690695&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 2021 Uchigashima, Cheung and Futai. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectautism (ASD)
dc.subjectcell adhension molecules
dc.subjectdevelopment
dc.subjectexcitatory synaptic activity
dc.subjectexcitatory/inhibitory balance
dc.subjectinhibitory synaptic connection
dc.subjectneuroligin 3 mutation
dc.subjecttrans-synaptic adhesion molecule
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectMolecular and Cellular Neuroscience
dc.subjectNervous System Diseases
dc.titleNeuroligin-3: A Circuit-Specific Synapse Organizer That Shapes Normal Function and Autism Spectrum Disorder-Associated Dysfunction
dc.typeJournal Article
dc.source.journaltitleFrontiers in molecular neuroscience
dc.source.volume14
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=3158&amp;context=faculty_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/faculty_pubs/2125
dc.identifier.contextkey26908864
refterms.dateFOA2022-08-23T15:56:14Z
html.description.abstract<p>Chemical synapses provide a vital foundation for neuron-neuron communication and overall brain function. By tethering closely apposed molecular machinery for presynaptic neurotransmitter release and postsynaptic signal transduction, circuit- and context- specific synaptic properties can drive neuronal computations for animal behavior. Trans-synaptic signaling via synaptic cell adhesion molecules (CAMs) serves as a promising mechanism to generate the molecular diversity of chemical synapses. Neuroligins (Nlgns) were discovered as postsynaptic CAMs that can bind to presynaptic CAMs like Neurexins (Nrxns) at the synaptic cleft. Among the four (Nlgn1-4) or five (Nlgn1-3, Nlgn4X, and Nlgn4Y) isoforms in rodents or humans, respectively, Nlgn3 has a heterogeneous expression and function at particular subsets of chemical synapses and strong association with non-syndromic autism spectrum disorder (ASD). Several lines of evidence have suggested that the unique expression and function of Nlgn3 protein underlie circuit-specific dysfunction characteristic of non-syndromic ASD caused by the disruption of Nlgn3 gene. Furthermore, recent studies have uncovered the molecular mechanism underlying input cell-dependent expression of Nlgn3 protein at hippocampal inhibitory synapses, in which trans-synaptic signaling of specific alternatively spliced isoforms of Nlgn3 and Nrxn plays a critical role. In this review article, we overview the molecular, anatomical, and physiological knowledge about Nlgn3, focusing on the circuit-specific function of mammalian Nlgn3 and its underlying molecular mechanism. This will provide not only new insight into specific Nlgn3-mediated trans-synaptic interactions as molecular codes for synapse specification but also a better understanding of the pathophysiological basis for non-syndromic ASD associated with functional impairment in Nlgn3 gene.</p>
dc.identifier.submissionpathfaculty_pubs/2125
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.contributor.departmentFutai Lab
dc.contributor.departmentBrudnick Neuropsychiatric Research Institute
dc.contributor.departmentNeurobiology
dc.source.pages749164
dc.contributor.studentAmy Cheung
dc.description.thesisprogramMD/PhD


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Copyright © 2021 Uchigashima, Cheung and Futai. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Except where otherwise noted, this item's license is described as Copyright © 2021 Uchigashima, Cheung and Futai. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.