DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
Authors
Mendoza-Topaz, CarolinaUrra, Francisco
Barria, Romina
Albornoz, Valeria
Ugalde, Diego
Thomas, Ulrich
Gundelfinger, Eckart
Delgado, Ricardo
Kukuljan, Manuel
Sanxaridis, Parthena D.
Tsunoda, Susan
Ceriani, M. Fernanda
Budnik, Vivian
Sierralta, Jimena
Document Type
Journal ArticlePublication Date
2008-01-02Keywords
AnimalsAnimals, Genetically Modified
Behavior, Animal
Circadian Rhythm
Drosophila
Drosophila Proteins
Embryo, Nonmammalian
Gene Expression Regulation, Developmental
Green Fluorescent Proteins
Membrane Potentials
Microscopy, Electron, Transmission
Motor Activity
Mutation
Neuromuscular Junction
Protein Isoforms
Sexual Behavior, Animal
Tumor Suppressor Proteins
Neuroscience and Neurobiology
Metadata
Show full item recordAbstract
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.Source
J Neurosci. 2008 Jan 2;28(1):304-14. Link to article on publisher's siteDOI
10.1523/JNEUROSCI.4395-07.2008Permanent Link to this Item
http://hdl.handle.net/20.500.14038/38007PubMed ID
18171947Related Resources
Link to Article in PubMedRights
Copyright 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 Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported license.ae974a485f413a2113503eed53cd6c53
10.1523/JNEUROSCI.4395-07.2008