To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor

Autores
Perillo, Vanesa Liliana; Peñalva, Daniel Alejandro; Aveldaño, Marta Isabel; Barrantes, Francisco Jose; Antollini, Silvia Susana
Año de publicación
2014
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
The preferential partitioning of the nicotinic acetylcholine receptor (AChR) in liquid-ordered (Lo) domains, heterogeneous membrane domains commonly known as rafts, is thought to be a part of its clustering mechanism. Previous studies from our group have shown that AChR lacks preference for Lo domains when reconstituted in sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model systems (Bermúdez et al., 2010). Here we study the effect on the possible Lo-preferential partitioning of purified AChR reconstituted in two different model systems (POPC:Chol, 1:1 and POPC:Chol:SM, 1:1:1) under: a) induced transbilayer asymmetry, resulting from addition of brain sphingomyelin (bSM) to the external hemilayer; and b) the presence of different pure SM species in the model membrane (bSM, 16:0-SM, 18:0-SM or 24:1-SM). AChR distribution was evaluated by fluorescence resonance energy transfer efficiency between the AChR intrinsic fluorescence and Laurdan or dehydroergosterol fluorescence, and also by determining the presence of AChR in detergent-resistant and detergent-soluble domains (1% Triton X- 100, 4°C). Both studies show that the induction of transbilayer asymmetry or the presence of 16:0-SM or 18:0-SM, as opposed to bSM or 24:1-SM, leads to a preferential partitioning of AChR in Lo domains. Thus, the localization of AChR in Lo domains strongly depends on the characteristics of the host lipid membrane
Fil: Perillo, Vanesa Liliana. 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: Peñalva, Daniel Alejandro. 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: Aveldaño, Marta Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto Argentino de Oceanografía. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; Argentina
Fil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Antollini, Silvia Susana. 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
Biophysical Society's 58th Annual Meeting
San Francisco
Estados Unidos
Biophysical Society
Materia
NICOTINIC ACETYLCHOLINE RECEPTOR
TRANSBILAYER ASYMMETRY
LIPID RAFTS
FLUORESCENCE SPECTROSCOPY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/246274
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/246274
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine ReceptorPerillo, Vanesa LilianaPeñalva, Daniel AlejandroAveldaño, Marta IsabelBarrantes, Francisco JoseAntollini, Silvia SusanaNICOTINIC ACETYLCHOLINE RECEPTORTRANSBILAYER ASYMMETRYLIPID RAFTSFLUORESCENCE SPECTROSCOPYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The preferential partitioning of the nicotinic acetylcholine receptor (AChR) in liquid-ordered (Lo) domains, heterogeneous membrane domains commonly known as rafts, is thought to be a part of its clustering mechanism. Previous studies from our group have shown that AChR lacks preference for Lo domains when reconstituted in sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model systems (Bermúdez et al., 2010). Here we study the effect on the possible Lo-preferential partitioning of purified AChR reconstituted in two different model systems (POPC:Chol, 1:1 and POPC:Chol:SM, 1:1:1) under: a) induced transbilayer asymmetry, resulting from addition of brain sphingomyelin (bSM) to the external hemilayer; and b) the presence of different pure SM species in the model membrane (bSM, 16:0-SM, 18:0-SM or 24:1-SM). AChR distribution was evaluated by fluorescence resonance energy transfer efficiency between the AChR intrinsic fluorescence and Laurdan or dehydroergosterol fluorescence, and also by determining the presence of AChR in detergent-resistant and detergent-soluble domains (1% Triton X- 100, 4°C). Both studies show that the induction of transbilayer asymmetry or the presence of 16:0-SM or 18:0-SM, as opposed to bSM or 24:1-SM, leads to a preferential partitioning of AChR in Lo domains. Thus, the localization of AChR in Lo domains strongly depends on the characteristics of the host lipid membraneFil: Perillo, Vanesa Liliana. 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: Peñalva, Daniel Alejandro. 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: Aveldaño, Marta Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto Argentino de Oceanografía. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; ArgentinaFil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; ArgentinaFil: Antollini, Silvia Susana. 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; ArgentinaBiophysical Society's 58th Annual MeetingSan FranciscoEstados UnidosBiophysical SocietyBiophysical Society2014info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/246274To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor; Biophysical Society's 58th Annual Meeting; San Francisco; Estados Unidos; 2014; 187-187CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.biophysics.org/Portals/0/EasyDNNnews/Uploads/2174/2014_Program_Guide.pdfInternacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:21:56Zoai:ri.conicet.gov.ar:11336/246274instacron: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 10:21:56.692CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
title To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
spellingShingle To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
Perillo, Vanesa Liliana
NICOTINIC ACETYLCHOLINE RECEPTOR
TRANSBILAYER ASYMMETRY
LIPID RAFTS
FLUORESCENCE SPECTROSCOPY
title_short To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
title_full To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
title_fullStr To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
title_full_unstemmed To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
title_sort To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor
dc.creator.none.fl_str_mv Perillo, Vanesa Liliana
Peñalva, Daniel Alejandro
Aveldaño, Marta Isabel
Barrantes, Francisco Jose
Antollini, Silvia Susana
author Perillo, Vanesa Liliana
author_facet Perillo, Vanesa Liliana
Peñalva, Daniel Alejandro
Aveldaño, Marta Isabel
Barrantes, Francisco Jose
Antollini, Silvia Susana
author_role author
author2 Peñalva, Daniel Alejandro
Aveldaño, Marta Isabel
Barrantes, Francisco Jose
Antollini, Silvia Susana
author2_role author
author
author
author
dc.subject.none.fl_str_mv NICOTINIC ACETYLCHOLINE RECEPTOR
TRANSBILAYER ASYMMETRY
LIPID RAFTS
FLUORESCENCE SPECTROSCOPY
topic NICOTINIC ACETYLCHOLINE RECEPTOR
TRANSBILAYER ASYMMETRY
LIPID RAFTS
FLUORESCENCE SPECTROSCOPY
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 preferential partitioning of the nicotinic acetylcholine receptor (AChR) in liquid-ordered (Lo) domains, heterogeneous membrane domains commonly known as rafts, is thought to be a part of its clustering mechanism. Previous studies from our group have shown that AChR lacks preference for Lo domains when reconstituted in sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model systems (Bermúdez et al., 2010). Here we study the effect on the possible Lo-preferential partitioning of purified AChR reconstituted in two different model systems (POPC:Chol, 1:1 and POPC:Chol:SM, 1:1:1) under: a) induced transbilayer asymmetry, resulting from addition of brain sphingomyelin (bSM) to the external hemilayer; and b) the presence of different pure SM species in the model membrane (bSM, 16:0-SM, 18:0-SM or 24:1-SM). AChR distribution was evaluated by fluorescence resonance energy transfer efficiency between the AChR intrinsic fluorescence and Laurdan or dehydroergosterol fluorescence, and also by determining the presence of AChR in detergent-resistant and detergent-soluble domains (1% Triton X- 100, 4°C). Both studies show that the induction of transbilayer asymmetry or the presence of 16:0-SM or 18:0-SM, as opposed to bSM or 24:1-SM, leads to a preferential partitioning of AChR in Lo domains. Thus, the localization of AChR in Lo domains strongly depends on the characteristics of the host lipid membrane
Fil: Perillo, Vanesa Liliana. 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: Peñalva, Daniel Alejandro. 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: Aveldaño, Marta Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto Argentino de Oceanografía. Universidad Nacional del Sur. Instituto Argentino de Oceanografía; Argentina
Fil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina
Fil: Antollini, Silvia Susana. 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
Biophysical Society's 58th Annual Meeting
San Francisco
Estados Unidos
Biophysical Society
description The preferential partitioning of the nicotinic acetylcholine receptor (AChR) in liquid-ordered (Lo) domains, heterogeneous membrane domains commonly known as rafts, is thought to be a part of its clustering mechanism. Previous studies from our group have shown that AChR lacks preference for Lo domains when reconstituted in sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model systems (Bermúdez et al., 2010). Here we study the effect on the possible Lo-preferential partitioning of purified AChR reconstituted in two different model systems (POPC:Chol, 1:1 and POPC:Chol:SM, 1:1:1) under: a) induced transbilayer asymmetry, resulting from addition of brain sphingomyelin (bSM) to the external hemilayer; and b) the presence of different pure SM species in the model membrane (bSM, 16:0-SM, 18:0-SM or 24:1-SM). AChR distribution was evaluated by fluorescence resonance energy transfer efficiency between the AChR intrinsic fluorescence and Laurdan or dehydroergosterol fluorescence, and also by determining the presence of AChR in detergent-resistant and detergent-soluble domains (1% Triton X- 100, 4°C). Both studies show that the induction of transbilayer asymmetry or the presence of 16:0-SM or 18:0-SM, as opposed to bSM or 24:1-SM, leads to a preferential partitioning of AChR in Lo domains. Thus, the localization of AChR in Lo domains strongly depends on the characteristics of the host lipid membrane
publishDate 2014
dc.date.none.fl_str_mv 2014
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Congreso
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/246274
To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor; Biophysical Society's 58th Annual Meeting; San Francisco; Estados Unidos; 2014; 187-187
CONICET Digital
CONICET
url http://hdl.handle.net/11336/246274
identifier_str_mv To be or not to be in Membrane Domains: Transbilayer Asymmetry and Sphingomyelin-Dependent Preferential Partitioning of the Acetylcholine Receptor; Biophysical Society's 58th Annual Meeting; San Francisco; Estados Unidos; 2014; 187-187
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://www.biophysics.org/Portals/0/EasyDNNnews/Uploads/2174/2014_Program_Guide.pdf
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.coverage.none.fl_str_mv Internacional
dc.publisher.none.fl_str_mv Biophysical Society
publisher.none.fl_str_mv Biophysical Society
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 13.070432

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