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dc.contributor.authorMendoza-Topaz, Carolina
dc.contributor.authorUrra, Francisco
dc.contributor.authorBarria, Romina
dc.contributor.authorAlbornoz, Valeria
dc.contributor.authorUgalde, Diego
dc.contributor.authorThomas, Ulrich
dc.contributor.authorGundelfinger, Eckart
dc.contributor.authorDelgado, Ricardo
dc.contributor.authorKukuljan, Manuel
dc.contributor.authorSanxaridis, Parthena D.
dc.contributor.authorTsunoda, Susan
dc.contributor.authorCeriani, M. Fernanda
dc.contributor.authorBudnik, Vivian
dc.contributor.authorSierralta, Jimena
dc.date2022-08-11T08:09:30.000
dc.date.accessioned2022-08-23T16:33:01Z
dc.date.available2022-08-23T16:33:01Z
dc.date.issued2008-01-02
dc.date.submitted2012-05-24
dc.identifier.citationJ Neurosci. 2008 Jan 2;28(1):304-14. <a href="http://dx.doi.org/10.1523/JNEUROSCI.4395-07.2008" target="_blank">Link to article on publisher's site</a>
dc.identifier.issn0270-6474 (Linking)
dc.identifier.doi10.1523/JNEUROSCI.4395-07.2008
dc.identifier.pmid18171947
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38007
dc.description.abstractThe synaptic membrane-associated guanylate kinase (MAGUK) scaffolding protein family is thought to play key roles in synapse assembly and synaptic plasticity. Evidence supporting these roles in vivo is scarce, as a consequence of gene redundancy in mammals. The genome of Drosophila contains only one MAGUK gene, discs large (dlg), from which two major proteins originate: DLGA [PSD95 (postsynaptic density 95)-like] and DLGS97 [SAP97 (synapse-associated protein)-like]. These differ only by the inclusion in DLGS97 of an L27 domain, important for the formation of supramolecular assemblies. Known dlg mutations affect both forms and are lethal at larval stages attributable to tumoral overgrowth of epithelia. We generated independent null mutations for each, dlgA and dlgS97. These allowed unveiling of a shift in expression during the development of the nervous system: predominant expression of DLGA in the embryo, balanced expression of both during larval stages, and almost exclusive DLGS97 expression in the adult brain. Loss of embryonic DLGS97 does not alter the development of the nervous system. At larval stages, DLGA and DLGS97 fulfill both unique and partially redundant functions in the neuromuscular junction. Contrary to dlg and dlgA mutants, dlgS97 mutants are viable to adulthood, but they exhibit marked alterations in complex behaviors such as phototaxis, circadian activity, and courtship, whereas simpler behaviors like locomotion and odor and light perception are spared. We propose that the increased repertoire of associations of a synaptic scaffold protein given by an additional domain of protein-protein interaction underlies its ability to integrate molecular networks required for complex functions in adult synapses.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=18171947&dopt=Abstract">Link to Article in PubMed</a>
dc.rightsCopyright of all material published in The Journal of Neuroscience remains with the authors. The authors grant the Society for Neuroscience an exclusive license to publish their work for the first 6 months. After 6 months the work becomes available to the public to copy, distribute, or display under a <a href="http://creativecommons.org/about/licenses">Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported license</a>.
dc.subjectAnimals
dc.subjectAnimals, Genetically Modified
dc.subjectBehavior, Animal
dc.subjectCircadian Rhythm
dc.subjectDrosophila
dc.subjectDrosophila Proteins
dc.subjectEmbryo, Nonmammalian
dc.subjectGene Expression Regulation, Developmental
dc.subjectGreen Fluorescent Proteins
dc.subjectMembrane Potentials
dc.subjectMicroscopy, Electron, Transmission
dc.subjectMotor Activity
dc.subjectMutation
dc.subjectNeuromuscular Junction
dc.subjectProtein Isoforms
dc.subjectSexual Behavior, Animal
dc.subjectTumor Suppressor Proteins
dc.subjectNeuroscience and Neurobiology
dc.titleDLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
dc.typeJournal Article
dc.source.journaltitleThe Journal of neuroscience : the official journal of the Society for Neuroscience
dc.source.volume28
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1039&amp;context=neurobiology_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/neurobiology_pp/40
dc.identifier.contextkey2911155
refterms.dateFOA2022-08-23T16:33:01Z
html.description.abstract<p>The synaptic membrane-associated guanylate kinase (MAGUK) scaffolding protein family is thought to play key roles in synapse assembly and synaptic plasticity. Evidence supporting these roles in vivo is scarce, as a consequence of gene redundancy in mammals. The genome of Drosophila contains only one MAGUK gene, discs large (dlg), from which two major proteins originate: DLGA [PSD95 (postsynaptic density 95)-like] and DLGS97 [SAP97 (synapse-associated protein)-like]. These differ only by the inclusion in DLGS97 of an L27 domain, important for the formation of supramolecular assemblies. Known dlg mutations affect both forms and are lethal at larval stages attributable to tumoral overgrowth of epithelia. We generated independent null mutations for each, dlgA and dlgS97. These allowed unveiling of a shift in expression during the development of the nervous system: predominant expression of DLGA in the embryo, balanced expression of both during larval stages, and almost exclusive DLGS97 expression in the adult brain. Loss of embryonic DLGS97 does not alter the development of the nervous system. At larval stages, DLGA and DLGS97 fulfill both unique and partially redundant functions in the neuromuscular junction. Contrary to dlg and dlgA mutants, dlgS97 mutants are viable to adulthood, but they exhibit marked alterations in complex behaviors such as phototaxis, circadian activity, and courtship, whereas simpler behaviors like locomotion and odor and light perception are spared. We propose that the increased repertoire of associations of a synaptic scaffold protein given by an additional domain of protein-protein interaction underlies its ability to integrate molecular networks required for complex functions in adult synapses.</p>
dc.identifier.submissionpathneurobiology_pp/40
dc.contributor.departmentBudnik Lab
dc.contributor.departmentNeurobiology
dc.source.pages304-14


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