Membrane Remodeling by Arc/Arg3.1

The activity-regulated cytoskeletal-associated protein (Arc, also known as Arg3.1) is an immediate early gene product induced by activity/experience and required for multiple modes of synaptic plasticity. Both long-term potentiation (LTP) and long-term depression (LTD) are impaired upon Arc deletion...

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Detalles Bibliográficos
Autores: Hedde, Per Niklas, Malacrida, Leonel, Barylko, Barbara, Binns, Derk D., Albanesi, Joseph P., Jameson, David M.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:Uruguay
Institución:Universidad de la República
Repositorio:COLIBRI
Idioma:inglés
OAI Identifier:oai:colibri.udelar.edu.uy:20.500.12008/55511
Acceso en línea:https://hdl.handle.net/20.500.12008/55511
Access Level:acceso abierto
Palabra clave:Arc
GUV
Giant unilamellar vesicle
Membrane remodeling
Fluorescence
Membrane budding
FLUORESCENCIA
MEMBRANA CELULAR
PROTEÍNAS
SISTEMA NERVIOSO
GENÉTICA
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dc.title.none.fl_str_mv Membrane Remodeling by Arc/Arg3.1
title Membrane Remodeling by Arc/Arg3.1
spellingShingle Membrane Remodeling by Arc/Arg3.1
Hedde, Per Niklas
Arc
GUV
Giant unilamellar vesicle
Membrane remodeling
Fluorescence
Membrane budding
FLUORESCENCIA
MEMBRANA CELULAR
PROTEÍNAS
SISTEMA NERVIOSO
GENÉTICA
title_short Membrane Remodeling by Arc/Arg3.1
title_full Membrane Remodeling by Arc/Arg3.1
title_fullStr Membrane Remodeling by Arc/Arg3.1
title_full_unstemmed Membrane Remodeling by Arc/Arg3.1
title_sort Membrane Remodeling by Arc/Arg3.1
dc.creator.none.fl_str_mv Hedde, Per Niklas
Malacrida, Leonel
Barylko, Barbara
Binns, Derk D.
Albanesi, Joseph P.
Jameson, David M.
author Hedde, Per Niklas
author_facet Hedde, Per Niklas
Malacrida, Leonel
Barylko, Barbara
Binns, Derk D.
Albanesi, Joseph P.
Jameson, David M.
author_role author
author2 Malacrida, Leonel
Barylko, Barbara
Binns, Derk D.
Albanesi, Joseph P.
Jameson, David M.
author2_role author
author
author
author
author
dc.contributor.filiacion.none.fl_str_mv Hedde Per Niklas, University of Hawaii at Manoa (E.E.U.U.). Department of Cell and Molecular Biology; University of California (E.E.U.U.). Laboratory for Fluorescence Dynamics
Malacrida Leonel, Universidad de la República (Uruguay). Facultad de Medicina. Hospital de Clínicas. Departamento de Fisiopatología; Institute Pasteur of Montevideo (Uruguay). Unidad de Bioimagenología Avanzada
Barylko Barbara, University of Texas Southwestern Medical Center (E.E.U.U.). Department of Pharmacology
Binns Derk D., University of Texas Southwestern Medical Center (E.E.U.U.). Department of Pharmacology
Albanesi Joseph P., University of Texas Southwestern Medical Center (E.E.U.U.). Department of Pharmacology
Jameson David M., University of Hawaii at Manoa (E.E.U.U.). Department of Cell and Molecular Biology
dc.subject.es.fl_str_mv Arc
GUV
Giant unilamellar vesicle
Membrane remodeling
Fluorescence
Membrane budding
topic Arc
GUV
Giant unilamellar vesicle
Membrane remodeling
Fluorescence
Membrane budding
FLUORESCENCIA
MEMBRANA CELULAR
PROTEÍNAS
SISTEMA NERVIOSO
GENÉTICA
dc.subject.other.es.fl_str_mv FLUORESCENCIA
MEMBRANA CELULAR
PROTEÍNAS
SISTEMA NERVIOSO
GENÉTICA
description The activity-regulated cytoskeletal-associated protein (Arc, also known as Arg3.1) is an immediate early gene product induced by activity/experience and required for multiple modes of synaptic plasticity. Both long-term potentiation (LTP) and long-term depression (LTD) are impaired upon Arc deletion, as well as the ability to form long-term spatial, taste and fear memories. The best-characterized cellular function of Arc is enhancement of the endocytic internalization of AMPA receptors (AMPARs) in dendritic spines. Solution of the crystal structure of a C-terminal segment of Arc revealed a striking similarity to the capsid domain of HIV Gag. It was subsequently shown that Arc assembles into viral capsid-like structures that enclose Arc mRNA, are released into the extracellular space, and are internalized by neighboring cells. Thus, Arc is unique in participating in plasma membrane budding both into and out of the cell. In this report we study the interaction of Arc with membranes using giant unilamellar vesicles (GUVs). Using the fluorescent lipid probe LAURDAN, we find that Arc promotes the formation of smaller vesicles that penetrate into the GUV interior. Our results suggest that Arc induces negative membrane curvature and may therefore facilitate the formation of mRNA-containing extracellular vesicles from the plasma membrane.
publishDate 2021
dc.date.issued.none.fl_str_mv 2021
dc.date.accessioned.none.fl_str_mv 2026-06-15T13:41:44Z
dc.date.available.none.fl_str_mv 2026-06-15T13:41:44Z
dc.type.es.fl_str_mv Artículo
dc.type.none.fl_str_mv info:eu-repo/semantics/article
dc.type.version.none.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.citation.es.fl_str_mv Hedde P, Malacrida L, Barylko B y otros. Membrane Remodeling by Arc/Arg3.1. Frontiers in Molecular Biosciences [en línea]. 2021;8 9 p.
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/20.500.12008/55511
dc.identifier.doi.none.fl_str_mv 10.3389/fmolb.2021.630625
dc.identifier.eissn.none.fl_str_mv 2296-889X
identifier_str_mv Hedde P, Malacrida L, Barylko B y otros. Membrane Remodeling by Arc/Arg3.1. Frontiers in Molecular Biosciences [en línea]. 2021;8 9 p.
10.3389/fmolb.2021.630625
2296-889X
url https://hdl.handle.net/20.500.12008/55511
dc.language.iso.none.fl_str_mv en
eng
language_invalid_str_mv en
language eng
dc.relation.none.fl_str_mv Frontiers in Molecular Biosciences. 2021;8
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.license.none.fl_str_mv Licencia Creative Commons Atribución (CC - By 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv Licencia Creative Commons Atribución (CC - By 4.0)
dc.format.extent.es.fl_str_mv 9 p.
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dc.publisher.es.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv reponame:COLIBRI
instname:Universidad de la República
instacron:Universidad de la República
instname_str Universidad de la República
instacron_str Universidad de la República
institution Universidad de la República
reponame_str COLIBRI
collection COLIBRI
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spelling Hedde Per Niklas, University of Hawaii at Manoa (E.E.U.U.). Department of Cell and Molecular Biology; University of California (E.E.U.U.). Laboratory for Fluorescence DynamicsMalacrida Leonel, Universidad de la República (Uruguay). Facultad de Medicina. Hospital de Clínicas. Departamento de Fisiopatología; Institute Pasteur of Montevideo (Uruguay). Unidad de Bioimagenología AvanzadaBarylko Barbara, University of Texas Southwestern Medical Center (E.E.U.U.). Department of PharmacologyBinns Derk D., University of Texas Southwestern Medical Center (E.E.U.U.). Department of PharmacologyAlbanesi Joseph P., University of Texas Southwestern Medical Center (E.E.U.U.). Department of PharmacologyJameson David M., University of Hawaii at Manoa (E.E.U.U.). Department of Cell and Molecular Biology2026-06-15T13:41:44Z2026-06-15T13:41:44Z2021Hedde P, Malacrida L, Barylko B y otros. Membrane Remodeling by Arc/Arg3.1. Frontiers in Molecular Biosciences [en línea]. 2021;8 9 p.https://hdl.handle.net/20.500.12008/5551110.3389/fmolb.2021.6306252296-889XThe activity-regulated cytoskeletal-associated protein (Arc, also known as Arg3.1) is an immediate early gene product induced by activity/experience and required for multiple modes of synaptic plasticity. Both long-term potentiation (LTP) and long-term depression (LTD) are impaired upon Arc deletion, as well as the ability to form long-term spatial, taste and fear memories. The best-characterized cellular function of Arc is enhancement of the endocytic internalization of AMPA receptors (AMPARs) in dendritic spines. Solution of the crystal structure of a C-terminal segment of Arc revealed a striking similarity to the capsid domain of HIV Gag. It was subsequently shown that Arc assembles into viral capsid-like structures that enclose Arc mRNA, are released into the extracellular space, and are internalized by neighboring cells. Thus, Arc is unique in participating in plasma membrane budding both into and out of the cell. In this report we study the interaction of Arc with membranes using giant unilamellar vesicles (GUVs). Using the fluorescent lipid probe LAURDAN, we find that Arc promotes the formation of smaller vesicles that penetrate into the GUV interior. Our results suggest that Arc induces negative membrane curvature and may therefore facilitate the formation of mRNA-containing extracellular vesicles from the plasma membrane.Submitted by Almiñana María Cecilia (marialminana@gmail.com) on 2026-06-12T16:03:34Z No. of bitstreams: 2 license_rdf: 25630 bytes, checksum: e7132498e7c1fe99f7096667baa99b25 (MD5) Membrane Remodeling.pdf: 4737186 bytes, checksum: b1e291adf988df475254a9a41b9cb7ba (MD5)Approved for entry into archive by Almiñana María Cecilia (marialminana@gmail.com) on 2026-06-15T11:09:20Z (GMT) No. of bitstreams: 2 license_rdf: 25630 bytes, checksum: e7132498e7c1fe99f7096667baa99b25 (MD5) Membrane Remodeling.pdf: 4737186 bytes, checksum: b1e291adf988df475254a9a41b9cb7ba (MD5)Made available in DSpace by Luna Fabiana (fabiana.luna@seciu.edu.uy) on 2026-06-15T13:41:44Z (GMT). No. of bitstreams: 2 license_rdf: 25630 bytes, checksum: e7132498e7c1fe99f7096667baa99b25 (MD5) Membrane Remodeling.pdf: 4737186 bytes, checksum: b1e291adf988df475254a9a41b9cb7ba (MD5) Previous issue date: 20219 p.application/pdfenengFrontiers MediaFrontiers in Molecular Biosciences. 2021;8Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)info:eu-repo/semantics/openAccessLicencia Creative Commons Atribución (CC - By 4.0)ArcGUVGiant unilamellar vesicleMembrane remodelingFluorescenceMembrane buddingFLUORESCENCIAMEMBRANA CELULARPROTEÍNASSISTEMA NERVIOSOGENÉTICAMembrane Remodeling by Arc/Arg3.1Artículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionreponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la RepúblicaHedde, Per NiklasMalacrida, LeonelBarylko, BarbaraBinns, Derk D.Albanesi, Joseph P.Jameson, David M.LICENSElicense.txtlicense.txttext/plain; charset=utf-84267http://localhost:8080/xmlui/bitstream/20.500.12008/55511/5/license.txt6429389a7df7277b72b7924fdc7d47a9MD55CC-LICENSElicense_urllicense_urltext/plain; charset=utf-844http://localhost:8080/xmlui/bitstream/20.500.12008/55511/2/license_urla0ebbeafb9d2ec7cbb19d7137ebc392cMD52license_textlicense_texttext/html; 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públicahttps://udelar.edu.uy/https://www.colibri.udelar.edu.uy/oai/requestkarina.camps@seciu.edu.uyUruguayopendoar:47712026-06-15T13:41:44COLIBRI - Universidad de la Repúblicafalse
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