Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization

Autores
Borroni, Maria Virginia; Barrantes, Francisco Jose
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Stability of the nicotinic acetylcholine receptor (AChR) at the cell surface is key to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is necessary for homeostasis of AChRlevels at the plasmalemma and for ion translocation. Here we characterize the endocytic pathway followed by muscle-type AChR in Chol-depleted cells (Chol-). Under such conditions, the AChR is internalized by a ligand-, clathrin-, and dynamin-independent mechanism. Expression of a dominant negative form of the small GTPase Rac1, Rac1N17, abolishes receptor endocytosis. Unlike the endocytic pathway in controlCHOcells (1), accelerated AChR internalization proceeds even upon disruption of the actin cytoskeleton. Under Chol- conditions, AChR internalization is furthermore found to require the activity of Arf6 and its effectors Rac1 and phospholipase D. The Arf6-dependent mechanism may constitute the default endocytic pathway followed by the AChR in the absence of external ligands, membrane Chol levels acting as a key homeostatic regulator of cell surface receptor levels.
Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Materia
CHOLESTEROL
NICOTINIC ACETYLCHOLINE RECEPTOR
ARF 6
ENDOCYTOSIS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/192186
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/192186
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cholesterol modulates the rate and mechanism of acetylcholine receptor internalizationBorroni, Maria VirginiaBarrantes, Francisco JoseCHOLESTEROLNICOTINIC ACETYLCHOLINE RECEPTORARF 6ENDOCYTOSIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Stability of the nicotinic acetylcholine receptor (AChR) at the cell surface is key to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is necessary for homeostasis of AChRlevels at the plasmalemma and for ion translocation. Here we characterize the endocytic pathway followed by muscle-type AChR in Chol-depleted cells (Chol-). Under such conditions, the AChR is internalized by a ligand-, clathrin-, and dynamin-independent mechanism. Expression of a dominant negative form of the small GTPase Rac1, Rac1N17, abolishes receptor endocytosis. Unlike the endocytic pathway in controlCHOcells (1), accelerated AChR internalization proceeds even upon disruption of the actin cytoskeleton. Under Chol- conditions, AChR internalization is furthermore found to require the activity of Arf6 and its effectors Rac1 and phospholipase D. The Arf6-dependent mechanism may constitute the default endocytic pathway followed by the AChR in the absence of external ligands, membrane Chol levels acting as a key homeostatic regulator of cell surface receptor levels.Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaAmerican Society for Biochemistry and Molecular Biology2011-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/192186Borroni, Maria Virginia; Barrantes, Francisco Jose; Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 286; 19; 5-2011; 17122-171320021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0021925820513434info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M110.211870info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:06Zoai:ri.conicet.gov.ar:11336/192186instacron: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 10:11:06.714CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
title Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
spellingShingle Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
Borroni, Maria Virginia
CHOLESTEROL
NICOTINIC ACETYLCHOLINE RECEPTOR
ARF 6
ENDOCYTOSIS
title_short Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
title_full Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
title_fullStr Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
title_full_unstemmed Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
title_sort Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization
dc.creator.none.fl_str_mv Borroni, Maria Virginia
Barrantes, Francisco Jose
author Borroni, Maria Virginia
author_facet Borroni, Maria Virginia
Barrantes, Francisco Jose
author_role author
author2 Barrantes, Francisco Jose
author2_role author
dc.subject.none.fl_str_mv CHOLESTEROL
NICOTINIC ACETYLCHOLINE RECEPTOR
ARF 6
ENDOCYTOSIS
topic CHOLESTEROL
NICOTINIC ACETYLCHOLINE RECEPTOR
ARF 6
ENDOCYTOSIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Stability of the nicotinic acetylcholine receptor (AChR) at the cell surface is key to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is necessary for homeostasis of AChRlevels at the plasmalemma and for ion translocation. Here we characterize the endocytic pathway followed by muscle-type AChR in Chol-depleted cells (Chol-). Under such conditions, the AChR is internalized by a ligand-, clathrin-, and dynamin-independent mechanism. Expression of a dominant negative form of the small GTPase Rac1, Rac1N17, abolishes receptor endocytosis. Unlike the endocytic pathway in controlCHOcells (1), accelerated AChR internalization proceeds even upon disruption of the actin cytoskeleton. Under Chol- conditions, AChR internalization is furthermore found to require the activity of Arf6 and its effectors Rac1 and phospholipase D. The Arf6-dependent mechanism may constitute the default endocytic pathway followed by the AChR in the absence of external ligands, membrane Chol levels acting as a key homeostatic regulator of cell surface receptor levels.
Fil: Borroni, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
description Stability of the nicotinic acetylcholine receptor (AChR) at the cell surface is key to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is necessary for homeostasis of AChRlevels at the plasmalemma and for ion translocation. Here we characterize the endocytic pathway followed by muscle-type AChR in Chol-depleted cells (Chol-). Under such conditions, the AChR is internalized by a ligand-, clathrin-, and dynamin-independent mechanism. Expression of a dominant negative form of the small GTPase Rac1, Rac1N17, abolishes receptor endocytosis. Unlike the endocytic pathway in controlCHOcells (1), accelerated AChR internalization proceeds even upon disruption of the actin cytoskeleton. Under Chol- conditions, AChR internalization is furthermore found to require the activity of Arf6 and its effectors Rac1 and phospholipase D. The Arf6-dependent mechanism may constitute the default endocytic pathway followed by the AChR in the absence of external ligands, membrane Chol levels acting as a key homeostatic regulator of cell surface receptor levels.
publishDate 2011
dc.date.none.fl_str_mv 2011-05
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/11336/192186
Borroni, Maria Virginia; Barrantes, Francisco Jose; Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 286; 19; 5-2011; 17122-17132
0021-9258
CONICET Digital
CONICET
url http://hdl.handle.net/11336/192186
identifier_str_mv Borroni, Maria Virginia; Barrantes, Francisco Jose; Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 286; 19; 5-2011; 17122-17132
0021-9258
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0021925820513434
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M110.211870
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
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 13.13397

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