DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function

Autores
Mendoza Topaz, Carolina; Urra, Francisco; Barría, Romina; Albornoz, Valeria; Ugalde, Diego; Thomas, Ulrich; Gundelfinger, Eckart D.; Delgado, Ricardo; Kukuljan, Manuel; Sanxaridis, Parthena D.; Tsunoda, Susan; Ceriani, Maria Fernanda; Budnik, Vivian; Sierralta, Jimena
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Mendoza Topaz, Carolina. Universidad de Chile; Chile
Fil: Urra, Francisco. Universidad de Chile; Chile
Fil: Barría, Romina. Universidad de Chile; Chile
Fil: Albornoz, Valeria. Universidad de Chile; Chile
Fil: Ugalde, Diego. Universidad de Chile; Chile
Fil: Thomas, Ulrich. Leibniz Institute for Neurobiology; Alemania
Fil: Gundelfinger, Eckart D.. Leibniz Institute for Neurobiology; Alemania
Fil: Delgado, Ricardo. Millenium Institute for Cell Dynamics and Biotechnology; Chile
Fil: Kukuljan, Manuel. Universidad de Chile; Chile
Fil: Sanxaridis, Parthena D.. Boston University; Estados Unidos
Fil: Tsunoda, Susan. Boston University; Estados Unidos
Fil: Ceriani, Maria Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Budnik, Vivian. University of Massachussets; Estados Unidos
Fil: Sierralta, Jimena. Universidad de Chile; Chile
Materia
SCAFFOLD PROTEINS
SYNAPSES
DROSOPHILA
BEHAVIOR
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/22699
Acceder
id CONICETDig_0752c8f904ccbac6732810b54cb9344f
oai_identifier_str oai:ri.conicet.gov.ar:11336/22699
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and functionMendoza Topaz, CarolinaUrra, FranciscoBarría, RominaAlbornoz, ValeriaUgalde, DiegoThomas, UlrichGundelfinger, Eckart D.Delgado, RicardoKukuljan, ManuelSanxaridis, Parthena D.Tsunoda, SusanCeriani, Maria FernandaBudnik, VivianSierralta, JimenaSCAFFOLD PROTEINSSYNAPSESDROSOPHILABEHAVIORhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 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.Fil: Mendoza Topaz, Carolina. Universidad de Chile; ChileFil: Urra, Francisco. Universidad de Chile; ChileFil: Barría, Romina. Universidad de Chile; ChileFil: Albornoz, Valeria. Universidad de Chile; ChileFil: Ugalde, Diego. Universidad de Chile; ChileFil: Thomas, Ulrich. Leibniz Institute for Neurobiology; AlemaniaFil: Gundelfinger, Eckart D.. Leibniz Institute for Neurobiology; AlemaniaFil: Delgado, Ricardo. Millenium Institute for Cell Dynamics and Biotechnology; ChileFil: Kukuljan, Manuel. Universidad de Chile; ChileFil: Sanxaridis, Parthena D.. Boston University; Estados UnidosFil: Tsunoda, Susan. Boston University; Estados UnidosFil: Ceriani, Maria Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Budnik, Vivian. University of Massachussets; Estados UnidosFil: Sierralta, Jimena. Universidad de Chile; ChileSociety for Neuroscience2008-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/22699Mendoza Topaz, Carolina; Urra, Francisco; Barría, Romina; Albornoz, Valeria; Ugalde, Diego; et al.; DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function; Society for Neuroscience; Journal of Neuroscience; 28; 1; 1-2008; 304-3140270-64741529-2401CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.jneurosci.org/content/28/1/304.longinfo:eu-repo/semantics/altIdentifier/doi/10.1523/JNEUROSCI.4395-07.2008info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:01:58Zoai:ri.conicet.gov.ar:11336/22699instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 12:01:58.511CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
title DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
spellingShingle DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
Mendoza Topaz, Carolina
SCAFFOLD PROTEINS
SYNAPSES
DROSOPHILA
BEHAVIOR
title_short DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
title_full DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
title_fullStr DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
title_full_unstemmed DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
title_sort DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function
dc.creator.none.fl_str_mv Mendoza Topaz, Carolina
Urra, Francisco
Barría, Romina
Albornoz, Valeria
Ugalde, Diego
Thomas, Ulrich
Gundelfinger, Eckart D.
Delgado, Ricardo
Kukuljan, Manuel
Sanxaridis, Parthena D.
Tsunoda, Susan
Ceriani, Maria Fernanda
Budnik, Vivian
Sierralta, Jimena
author Mendoza Topaz, Carolina
author_facet Mendoza Topaz, Carolina
Urra, Francisco
Barría, Romina
Albornoz, Valeria
Ugalde, Diego
Thomas, Ulrich
Gundelfinger, Eckart D.
Delgado, Ricardo
Kukuljan, Manuel
Sanxaridis, Parthena D.
Tsunoda, Susan
Ceriani, Maria Fernanda
Budnik, Vivian
Sierralta, Jimena
author_role author
author2 Urra, Francisco
Barría, Romina
Albornoz, Valeria
Ugalde, Diego
Thomas, Ulrich
Gundelfinger, Eckart D.
Delgado, Ricardo
Kukuljan, Manuel
Sanxaridis, Parthena D.
Tsunoda, Susan
Ceriani, Maria Fernanda
Budnik, Vivian
Sierralta, Jimena
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv SCAFFOLD PROTEINS
SYNAPSES
DROSOPHILA
BEHAVIOR
topic SCAFFOLD PROTEINS
SYNAPSES
DROSOPHILA
BEHAVIOR
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Mendoza Topaz, Carolina. Universidad de Chile; Chile
Fil: Urra, Francisco. Universidad de Chile; Chile
Fil: Barría, Romina. Universidad de Chile; Chile
Fil: Albornoz, Valeria. Universidad de Chile; Chile
Fil: Ugalde, Diego. Universidad de Chile; Chile
Fil: Thomas, Ulrich. Leibniz Institute for Neurobiology; Alemania
Fil: Gundelfinger, Eckart D.. Leibniz Institute for Neurobiology; Alemania
Fil: Delgado, Ricardo. Millenium Institute for Cell Dynamics and Biotechnology; Chile
Fil: Kukuljan, Manuel. Universidad de Chile; Chile
Fil: Sanxaridis, Parthena D.. Boston University; Estados Unidos
Fil: Tsunoda, Susan. Boston University; Estados Unidos
Fil: Ceriani, Maria Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Budnik, Vivian. University of Massachussets; Estados Unidos
Fil: Sierralta, Jimena. Universidad de Chile; Chile
description 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.
publishDate 2008
dc.date.none.fl_str_mv 2008-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/22699
Mendoza Topaz, Carolina; Urra, Francisco; Barría, Romina; Albornoz, Valeria; Ugalde, Diego; et al.; DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function; Society for Neuroscience; Journal of Neuroscience; 28; 1; 1-2008; 304-314
0270-6474
1529-2401
CONICET Digital
CONICET
url http://hdl.handle.net/11336/22699
identifier_str_mv Mendoza Topaz, Carolina; Urra, Francisco; Barría, Romina; Albornoz, Valeria; Ugalde, Diego; et al.; DLGS97/SAP97 is developmentally upregulated and is required for complex adult behaviors and synapse morphology and function; Society for Neuroscience; Journal of Neuroscience; 28; 1; 1-2008; 304-314
0270-6474
1529-2401
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jneurosci.org/content/28/1/304.long
info:eu-repo/semantics/altIdentifier/doi/10.1523/JNEUROSCI.4395-07.2008
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Society for Neuroscience
publisher.none.fl_str_mv Society for Neuroscience
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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