Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor
- Autores
- Borroni, Maria Virginia; Barrantes, Francisco Jose
- Año de publicación
- 2010
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- Stability of the nicotinic acetylcholine receptor (AChR) at the cell surface is critical to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is an essential lipid that modulates AChR. We have studied the endocytosis of AChR in CHO-K1/A5 cells, a cell line heterologously expressing murine muscle adulttype receptor under different Chol membrane contents. Contrary to the norm, endocytosis of cell-surface AChR is accelerated by depletion of membrane Chol. This acceleration is no longer operative when membrane Chol levels are restored. We explored the possible mechanism involved in receptor loss in Chol depleted cells (Chol-). Under such conditions the AChR is internalized by a ligand-, clathrin- and dynamin independent mechanism, which does not involve the presence of the AChR-associated protein rapsyn. The small GTPase Rac1 is required: expression of a dominant negative form of Rac1, Rac1N17, abrogates receptor endocytosis. The accelerated internalization of AChR proceeds even upon disruption of the actin cytoskeleton and is furthermore found to require the activity of the small GTPase Arf6 and its effectors Rac1 and phospholipase D. Thus, membrane Chol appears to act as a key homeostatic regulator of cell-surface receptor levels, determining not only the rate but also the mechanism of AChR endocytosis
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
46 Annual Meeting Argentine Society for Biochemistry and Molecular Biology
Puerto Madryn
Argentina
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular - Materia
-
CHOLESTEROL
CYTOSKELETON
ACETYLCHOLINE RECEPTOR
ENDOCYTOSIS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/232208
Ver los metadatos del registro completo
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Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine ReceptorBorroni, Maria VirginiaBarrantes, Francisco JoseCHOLESTEROLCYTOSKELETONACETYLCHOLINE RECEPTORENDOCYTOSIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Stability of the nicotinic acetylcholine receptor (AChR) at the cell surface is critical to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is an essential lipid that modulates AChR. We have studied the endocytosis of AChR in CHO-K1/A5 cells, a cell line heterologously expressing murine muscle adulttype receptor under different Chol membrane contents. Contrary to the norm, endocytosis of cell-surface AChR is accelerated by depletion of membrane Chol. This acceleration is no longer operative when membrane Chol levels are restored. We explored the possible mechanism involved in receptor loss in Chol depleted cells (Chol-). Under such conditions the AChR is internalized by a ligand-, clathrin- and dynamin independent mechanism, which does not involve the presence of the AChR-associated protein rapsyn. The small GTPase Rac1 is required: expression of a dominant negative form of Rac1, Rac1N17, abrogates receptor endocytosis. The accelerated internalization of AChR proceeds even upon disruption of the actin cytoskeleton and is furthermore found to require the activity of the small GTPase Arf6 and its effectors Rac1 and phospholipase D. Thus, membrane Chol appears to act as a key homeostatic regulator of cell-surface receptor levels, determining not only the rate but also the mechanism of AChR endocytosisFil: 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; Argentina46 Annual Meeting Argentine Society for Biochemistry and Molecular BiologyPuerto MadrynArgentinaSociedad Argentina de Investigación en Bioquímica y Biología MolecularSociedad Argentina de Investigación en Bioquímica y Biología Molecular2010info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/232208Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor; 46 Annual Meeting Argentine Society for Biochemistry and Molecular Biology; Puerto Madryn; Argentina; 2010; 69-690327-95451667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://saib.org.ar/archivos/biocell-34.pdfNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:42:57Zoai:ri.conicet.gov.ar:11336/232208instacron: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 09:42:57.685CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor |
| title |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor |
| spellingShingle |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor Borroni, Maria Virginia CHOLESTEROL CYTOSKELETON ACETYLCHOLINE RECEPTOR ENDOCYTOSIS |
| title_short |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor |
| title_full |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor |
| title_fullStr |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor |
| title_full_unstemmed |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor |
| title_sort |
Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor |
| 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 CYTOSKELETON ACETYLCHOLINE RECEPTOR ENDOCYTOSIS |
| topic |
CHOLESTEROL CYTOSKELETON ACETYLCHOLINE RECEPTOR 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 critical to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is an essential lipid that modulates AChR. We have studied the endocytosis of AChR in CHO-K1/A5 cells, a cell line heterologously expressing murine muscle adulttype receptor under different Chol membrane contents. Contrary to the norm, endocytosis of cell-surface AChR is accelerated by depletion of membrane Chol. This acceleration is no longer operative when membrane Chol levels are restored. We explored the possible mechanism involved in receptor loss in Chol depleted cells (Chol-). Under such conditions the AChR is internalized by a ligand-, clathrin- and dynamin independent mechanism, which does not involve the presence of the AChR-associated protein rapsyn. The small GTPase Rac1 is required: expression of a dominant negative form of Rac1, Rac1N17, abrogates receptor endocytosis. The accelerated internalization of AChR proceeds even upon disruption of the actin cytoskeleton and is furthermore found to require the activity of the small GTPase Arf6 and its effectors Rac1 and phospholipase D. Thus, membrane Chol appears to act as a key homeostatic regulator of cell-surface receptor levels, determining not only the rate but also the mechanism of AChR endocytosis 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 46 Annual Meeting Argentine Society for Biochemistry and Molecular Biology Puerto Madryn Argentina Sociedad Argentina de Investigación en Bioquímica y Biología Molecular |
| description |
Stability of the nicotinic acetylcholine receptor (AChR) at the cell surface is critical to the correct functioning of the cholinergic synapse. Cholesterol (Chol) is an essential lipid that modulates AChR. We have studied the endocytosis of AChR in CHO-K1/A5 cells, a cell line heterologously expressing murine muscle adulttype receptor under different Chol membrane contents. Contrary to the norm, endocytosis of cell-surface AChR is accelerated by depletion of membrane Chol. This acceleration is no longer operative when membrane Chol levels are restored. We explored the possible mechanism involved in receptor loss in Chol depleted cells (Chol-). Under such conditions the AChR is internalized by a ligand-, clathrin- and dynamin independent mechanism, which does not involve the presence of the AChR-associated protein rapsyn. The small GTPase Rac1 is required: expression of a dominant negative form of Rac1, Rac1N17, abrogates receptor endocytosis. The accelerated internalization of AChR proceeds even upon disruption of the actin cytoskeleton and is furthermore found to require the activity of the small GTPase Arf6 and its effectors Rac1 and phospholipase D. Thus, membrane Chol appears to act as a key homeostatic regulator of cell-surface receptor levels, determining not only the rate but also the mechanism of AChR endocytosis |
| publishDate |
2010 |
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2010 |
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http://hdl.handle.net/11336/232208 Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor; 46 Annual Meeting Argentine Society for Biochemistry and Molecular Biology; Puerto Madryn; Argentina; 2010; 69-69 0327-9545 1667-5746 CONICET Digital CONICET |
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Cholesterol Levels Determine The Endocytic Route Followed By The Acetylcholine Receptor; 46 Annual Meeting Argentine Society for Biochemistry and Molecular Biology; Puerto Madryn; Argentina; 2010; 69-69 0327-9545 1667-5746 CONICET Digital CONICET |
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eng |
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eng |
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Sociedad Argentina de Investigación en Bioquímica y Biología Molecular |
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Sociedad Argentina de Investigación en Bioquímica y Biología Molecular |
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