Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol

Autores
Barrantes, Francisco Jose
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cholesterol is a major lipid in biological membranes. It not only plays a structural role but also modulates a wide range of functional properties of neurotransmitter and hormone receptors and ion channels. The membraneembedded segments of the paradigm neurotransmitter receptor for acetylcholine (nAChR) contain linear sequences of amino acids with the capacity to recognize cholesterol. These cholesterol consensus domains have been designated as "CARC" and its mirror sequence "CRAC". CARC preferentially occurs in the exoplasmic-facing membrane leaflet, and CRAC, in the cytoplasmic-facing hemilayer. Both motifs are highly conserved among ion-channel and neurotransmitter receptor proteins in vertebrate nervous systems, where they recognize cholesterol, and in prokaryotic homologues in bacteria, where they recognize hopanoids. This phylogenetically conserved trait is an indication that the hopanoids in some bacteria and cholesterol in eukaryotes subserve analogous functions, probably contributing to the stability of membrane-embedded protein domains. Structural studies from our laboratory using superresolution optical microscopy ("nanoscopy") have disclosed other interrelated functional and structural properties exerted by cholesterol on the nAChR. The neutral lipid content at the cell surface influences both the macromolecular organization of the receptor and its translational mobility (diffusion) in the plane of the membrane.
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; Argentina
Materia
CHOLESTEROL
CHOLESTEROL-RECOGNITION DOMAINS
EVOLUTION
MEMBRANE PROTEINS
NANOSCOPY
NICOTINIC ACETYLCHOLINE RECEPTOR
PENTAMERIC LIGAND-GATED ION CHANNEL
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:11336/169081
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/169081
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterolBarrantes, Francisco JoseCHOLESTEROLCHOLESTEROL-RECOGNITION DOMAINSEVOLUTIONMEMBRANE PROTEINSNANOSCOPYNICOTINIC ACETYLCHOLINE RECEPTORPENTAMERIC LIGAND-GATED ION CHANNELhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cholesterol is a major lipid in biological membranes. It not only plays a structural role but also modulates a wide range of functional properties of neurotransmitter and hormone receptors and ion channels. The membraneembedded segments of the paradigm neurotransmitter receptor for acetylcholine (nAChR) contain linear sequences of amino acids with the capacity to recognize cholesterol. These cholesterol consensus domains have been designated as "CARC" and its mirror sequence "CRAC". CARC preferentially occurs in the exoplasmic-facing membrane leaflet, and CRAC, in the cytoplasmic-facing hemilayer. Both motifs are highly conserved among ion-channel and neurotransmitter receptor proteins in vertebrate nervous systems, where they recognize cholesterol, and in prokaryotic homologues in bacteria, where they recognize hopanoids. This phylogenetically conserved trait is an indication that the hopanoids in some bacteria and cholesterol in eukaryotes subserve analogous functions, probably contributing to the stability of membrane-embedded protein domains. Structural studies from our laboratory using superresolution optical microscopy ("nanoscopy") have disclosed other interrelated functional and structural properties exerted by cholesterol on the nAChR. The neutral lipid content at the cell surface influences both the macromolecular organization of the receptor and its translational mobility (diffusion) in the plane of the membrane.Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; ArgentinaInstituto de Histología y Embriología2021-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/169081Barrantes, Francisco Jose; Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol; Instituto de Histología y Embriología; Biocell; 45; 6; 6-2021; 1479-14840327-9545CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.32604/biocell.2021.016502info:eu-repo/semantics/altIdentifier/url/https://www.techscience.com/biocell/v45n6/44279info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:05:28Zoai:ri.conicet.gov.ar:11336/169081instacron: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 10:05:28.602CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
title Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
spellingShingle Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
Barrantes, Francisco Jose
CHOLESTEROL
CHOLESTEROL-RECOGNITION DOMAINS
EVOLUTION
MEMBRANE PROTEINS
NANOSCOPY
NICOTINIC ACETYLCHOLINE RECEPTOR
PENTAMERIC LIGAND-GATED ION CHANNEL
title_short Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
title_full Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
title_fullStr Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
title_full_unstemmed Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
title_sort Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol
dc.creator.none.fl_str_mv Barrantes, Francisco Jose
author Barrantes, Francisco Jose
author_facet Barrantes, Francisco Jose
author_role author
dc.subject.none.fl_str_mv CHOLESTEROL
CHOLESTEROL-RECOGNITION DOMAINS
EVOLUTION
MEMBRANE PROTEINS
NANOSCOPY
NICOTINIC ACETYLCHOLINE RECEPTOR
PENTAMERIC LIGAND-GATED ION CHANNEL
topic CHOLESTEROL
CHOLESTEROL-RECOGNITION DOMAINS
EVOLUTION
MEMBRANE PROTEINS
NANOSCOPY
NICOTINIC ACETYLCHOLINE RECEPTOR
PENTAMERIC LIGAND-GATED ION CHANNEL
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Cholesterol is a major lipid in biological membranes. It not only plays a structural role but also modulates a wide range of functional properties of neurotransmitter and hormone receptors and ion channels. The membraneembedded segments of the paradigm neurotransmitter receptor for acetylcholine (nAChR) contain linear sequences of amino acids with the capacity to recognize cholesterol. These cholesterol consensus domains have been designated as "CARC" and its mirror sequence "CRAC". CARC preferentially occurs in the exoplasmic-facing membrane leaflet, and CRAC, in the cytoplasmic-facing hemilayer. Both motifs are highly conserved among ion-channel and neurotransmitter receptor proteins in vertebrate nervous systems, where they recognize cholesterol, and in prokaryotic homologues in bacteria, where they recognize hopanoids. This phylogenetically conserved trait is an indication that the hopanoids in some bacteria and cholesterol in eukaryotes subserve analogous functions, probably contributing to the stability of membrane-embedded protein domains. Structural studies from our laboratory using superresolution optical microscopy ("nanoscopy") have disclosed other interrelated functional and structural properties exerted by cholesterol on the nAChR. The neutral lipid content at the cell surface influences both the macromolecular organization of the receptor and its translational mobility (diffusion) in the plane of the membrane.
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; Argentina
description Cholesterol is a major lipid in biological membranes. It not only plays a structural role but also modulates a wide range of functional properties of neurotransmitter and hormone receptors and ion channels. The membraneembedded segments of the paradigm neurotransmitter receptor for acetylcholine (nAChR) contain linear sequences of amino acids with the capacity to recognize cholesterol. These cholesterol consensus domains have been designated as "CARC" and its mirror sequence "CRAC". CARC preferentially occurs in the exoplasmic-facing membrane leaflet, and CRAC, in the cytoplasmic-facing hemilayer. Both motifs are highly conserved among ion-channel and neurotransmitter receptor proteins in vertebrate nervous systems, where they recognize cholesterol, and in prokaryotic homologues in bacteria, where they recognize hopanoids. This phylogenetically conserved trait is an indication that the hopanoids in some bacteria and cholesterol in eukaryotes subserve analogous functions, probably contributing to the stability of membrane-embedded protein domains. Structural studies from our laboratory using superresolution optical microscopy ("nanoscopy") have disclosed other interrelated functional and structural properties exerted by cholesterol on the nAChR. The neutral lipid content at the cell surface influences both the macromolecular organization of the receptor and its translational mobility (diffusion) in the plane of the membrane.
publishDate 2021
dc.date.none.fl_str_mv 2021-06
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/11336/169081
Barrantes, Francisco Jose; Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol; Instituto de Histología y Embriología; Biocell; 45; 6; 6-2021; 1479-1484
0327-9545
CONICET Digital
CONICET
url http://hdl.handle.net/11336/169081
identifier_str_mv Barrantes, Francisco Jose; Nanoscale interactions between the nicotinic acetylcholine receptor and cholesterol; Instituto de Histología y Embriología; Biocell; 45; 6; 6-2021; 1479-1484
0327-9545
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.32604/biocell.2021.016502
info:eu-repo/semantics/altIdentifier/url/https://www.techscience.com/biocell/v45n6/44279
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 Instituto de Histología y Embriología
publisher.none.fl_str_mv Instituto de Histología y Embriología
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
_version_ 1842269911883186176
score 13.13397

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