Chaperoning a7 neuronal nicotinic acetylcholine receptors

Autores
Valles, Ana Sofia; Barrantes, Francisco Jose
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The α7 subtype of nicotinic acetylcholine receptors (AChRs) is one of the most abundant members of the Cysloop family of receptors present in the central nervous system. It participates in various physiological processes and has received much attention as a potential therapeutic target for a variety of pathologies. The importance of understanding the mechanisms controlling AChR assembly and cell-surface delivery lies in the fact that these two processes are key to determining the functional pool of receptors actively engaged in synaptic transmission. Here we review recent studies showing that RIC-3, a protein originally identified in the worm Caenorhabditis elegans, modulates the expression of α7 AChRs in a subtype-specific manner. Potentiation of AChR expression by post-transcriptional events is also critically assessed.
Fil: Valles, Ana Sofia. Consejo Nacional de Investigaciones Cientificas y Técnicas. Centro Científico Tecnológico Bahia Blanca. Instituto de Investigaciones Bioquímicas Bahia Blanca (i); Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Cientificas y Técnicas. Centro Científico Tecnológico Bahia Blanca. Instituto de Investigaciones Bioquímicas Bahia Blanca (i); Argentina. Pontificia Universidad Católica "Santa María de Los Buenos Aires"; Argentina
Materia
Ric-3 Protein
Neuronal Nicotinic Achr
Receptor Traffiking
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/7076

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network_name_str CONICET Digital (CONICET)
spelling Chaperoning a7 neuronal nicotinic acetylcholine receptorsValles, Ana SofiaBarrantes, Francisco JoseRic-3 ProteinNeuronal Nicotinic AchrReceptor Traffikinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The α7 subtype of nicotinic acetylcholine receptors (AChRs) is one of the most abundant members of the Cysloop family of receptors present in the central nervous system. It participates in various physiological processes and has received much attention as a potential therapeutic target for a variety of pathologies. The importance of understanding the mechanisms controlling AChR assembly and cell-surface delivery lies in the fact that these two processes are key to determining the functional pool of receptors actively engaged in synaptic transmission. Here we review recent studies showing that RIC-3, a protein originally identified in the worm Caenorhabditis elegans, modulates the expression of α7 AChRs in a subtype-specific manner. Potentiation of AChR expression by post-transcriptional events is also critically assessed.Fil: Valles, Ana Sofia. Consejo Nacional de Investigaciones Cientificas y Técnicas. Centro Científico Tecnológico Bahia Blanca. Instituto de Investigaciones Bioquímicas Bahia Blanca (i); ArgentinaFil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Cientificas y Técnicas. Centro Científico Tecnológico Bahia Blanca. Instituto de Investigaciones Bioquímicas Bahia Blanca (i); Argentina. Pontificia Universidad Católica "Santa María de Los Buenos Aires"; ArgentinaElsevier2012-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/7076Valles, Ana Sofia; Barrantes, Francisco Jose; Chaperoning a7 neuronal nicotinic acetylcholine receptors; Elsevier; Biochimica Et Biophysica Acta - Biomembranes; 1818; 3; 3-2012; 718-7290005-2736enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273611003622info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2011.10.012info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:07:27Zoai:ri.conicet.gov.ar:11336/7076instacron: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:34982025-09-03 10:07:27.693CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Chaperoning a7 neuronal nicotinic acetylcholine receptors
title Chaperoning a7 neuronal nicotinic acetylcholine receptors
spellingShingle Chaperoning a7 neuronal nicotinic acetylcholine receptors
Valles, Ana Sofia
Ric-3 Protein
Neuronal Nicotinic Achr
Receptor Traffiking
title_short Chaperoning a7 neuronal nicotinic acetylcholine receptors
title_full Chaperoning a7 neuronal nicotinic acetylcholine receptors
title_fullStr Chaperoning a7 neuronal nicotinic acetylcholine receptors
title_full_unstemmed Chaperoning a7 neuronal nicotinic acetylcholine receptors
title_sort Chaperoning a7 neuronal nicotinic acetylcholine receptors
dc.creator.none.fl_str_mv Valles, Ana Sofia
Barrantes, Francisco Jose
author Valles, Ana Sofia
author_facet Valles, Ana Sofia
Barrantes, Francisco Jose
author_role author
author2 Barrantes, Francisco Jose
author2_role author
dc.subject.none.fl_str_mv Ric-3 Protein
Neuronal Nicotinic Achr
Receptor Traffiking
topic Ric-3 Protein
Neuronal Nicotinic Achr
Receptor Traffiking
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 α7 subtype of nicotinic acetylcholine receptors (AChRs) is one of the most abundant members of the Cysloop family of receptors present in the central nervous system. It participates in various physiological processes and has received much attention as a potential therapeutic target for a variety of pathologies. The importance of understanding the mechanisms controlling AChR assembly and cell-surface delivery lies in the fact that these two processes are key to determining the functional pool of receptors actively engaged in synaptic transmission. Here we review recent studies showing that RIC-3, a protein originally identified in the worm Caenorhabditis elegans, modulates the expression of α7 AChRs in a subtype-specific manner. Potentiation of AChR expression by post-transcriptional events is also critically assessed.
Fil: Valles, Ana Sofia. Consejo Nacional de Investigaciones Cientificas y Técnicas. Centro Científico Tecnológico Bahia Blanca. Instituto de Investigaciones Bioquímicas Bahia Blanca (i); Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Cientificas y Técnicas. Centro Científico Tecnológico Bahia Blanca. Instituto de Investigaciones Bioquímicas Bahia Blanca (i); Argentina. Pontificia Universidad Católica "Santa María de Los Buenos Aires"; Argentina
description The α7 subtype of nicotinic acetylcholine receptors (AChRs) is one of the most abundant members of the Cysloop family of receptors present in the central nervous system. It participates in various physiological processes and has received much attention as a potential therapeutic target for a variety of pathologies. The importance of understanding the mechanisms controlling AChR assembly and cell-surface delivery lies in the fact that these two processes are key to determining the functional pool of receptors actively engaged in synaptic transmission. Here we review recent studies showing that RIC-3, a protein originally identified in the worm Caenorhabditis elegans, modulates the expression of α7 AChRs in a subtype-specific manner. Potentiation of AChR expression by post-transcriptional events is also critically assessed.
publishDate 2012
dc.date.none.fl_str_mv 2012-03
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/11336/7076
Valles, Ana Sofia; Barrantes, Francisco Jose; Chaperoning a7 neuronal nicotinic acetylcholine receptors; Elsevier; Biochimica Et Biophysica Acta - Biomembranes; 1818; 3; 3-2012; 718-729
0005-2736
url http://hdl.handle.net/11336/7076
identifier_str_mv Valles, Ana Sofia; Barrantes, Francisco Jose; Chaperoning a7 neuronal nicotinic acetylcholine receptors; Elsevier; Biochimica Et Biophysica Acta - Biomembranes; 1818; 3; 3-2012; 718-729
0005-2736
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273611003622
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2011.10.012
info:eu-repo/semantics/altIdentifier/doi/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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