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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/7076
Ver los metadatos del registro completo
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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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13.13397 |