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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/22699
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:29:32Zoai: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:34982025-09-29 10:29:32.826CONICET 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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1844614302078599168 |
score |
13.070432 |