Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor

Autores
Baier, Carlos J.; Fantini, Jacques; Barrantes, Francisco José
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Baier, Carlos J. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Baier, Carlos J. Pontificia Universidad Católica Argentina. Programa de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentina
Fil: Baier, Carlos J. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fantini, Jacques. Université Paul Cézanne; Francia
Fil: Fantini, Jacques. Université de la Méditerrané, Centre de Recherche en Neurobiologie et Neurophysiologie de Marseille; Francia
Fil: Barrantes, Francisco J. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Barrantes, Francisco J. Instituto de Investigaciones Bioquímicas de Bahíaa Blanca; Argentina
Fil: Barrantes, Francisco J. United Nations Educational, Scientific and Cultural Organization. Chair of Biophysics and Molecular Neurobiology; Francia
Abstract: Cholesterol influences ion-channel function, distribution and clustering in the membrane, endocytosis, and exocytic sorting of the nicotinic acetylcholine receptor (AChR). We report the occurrence of a cholesterol recognition motif, here coined ‘‘CARC’’, in the transmembrane regions of AChR subunits that bear extensive contact with the surrounding lipid, and are thus optimally suited to convey cholesterol-mediated signaling from the latter. Three cholesterol molecules could be docked on the transmembrane segments of each AChR subunit, rendering a total of 15 cholesterol molecules per AChR molecule. The CARC motifs contribute each with an energy of interaction between 35 and 52 kJ.mol21, adding up to a total of about 200 kJ.mol21 per receptor molecule, i.e. 40% of the lipid solvation free energy/ AChR molecule. The CARC motif is remarkably conserved along the phylogenetic scale, from prokaryotes to human, suggesting that it could be responsible for some of the above structural/functional properties of the AChR.
Fuente
Scientific Reports. 2011, 1 (69)
Materia
COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
Repositorio Institucional (UCA)
Institución
Pontificia Universidad Católica Argentina
OAI Identificador
oai:ucacris:123456789/1462
Acceder
id RIUCA_624d19e40f61431b53429019c6540332
oai_identifier_str oai:ucacris:123456789/1462
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
spelling Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptorBaier, Carlos J.Fantini, JacquesBarrantes, Francisco JoséCOLESTEROLLIPIDOSCANALES IONICOSNEUROCIENCIAACHRNEUROBIOLOGIA MOLECULARFil: Baier, Carlos J. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; ArgentinaFil: Baier, Carlos J. Pontificia Universidad Católica Argentina. Programa de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; ArgentinaFil: Baier, Carlos J. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Fantini, Jacques. Université Paul Cézanne; FranciaFil: Fantini, Jacques. Université de la Méditerrané, Centre de Recherche en Neurobiologie et Neurophysiologie de Marseille; FranciaFil: Barrantes, Francisco J. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; ArgentinaFil: Barrantes, Francisco J. Instituto de Investigaciones Bioquímicas de Bahíaa Blanca; ArgentinaFil: Barrantes, Francisco J. United Nations Educational, Scientific and Cultural Organization. Chair of Biophysics and Molecular Neurobiology; FranciaAbstract: Cholesterol influences ion-channel function, distribution and clustering in the membrane, endocytosis, and exocytic sorting of the nicotinic acetylcholine receptor (AChR). We report the occurrence of a cholesterol recognition motif, here coined ‘‘CARC’’, in the transmembrane regions of AChR subunits that bear extensive contact with the surrounding lipid, and are thus optimally suited to convey cholesterol-mediated signaling from the latter. Three cholesterol molecules could be docked on the transmembrane segments of each AChR subunit, rendering a total of 15 cholesterol molecules per AChR molecule. The CARC motifs contribute each with an energy of interaction between 35 and 52 kJ.mol21, adding up to a total of about 200 kJ.mol21 per receptor molecule, i.e. 40% of the lipid solvation free energy/ AChR molecule. The CARC motif is remarkably conserved along the phylogenetic scale, from prokaryotes to human, suggesting that it could be responsible for some of the above structural/functional properties of the AChR.Nature Research2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/14622045-232210.1038/srep0006922355588Baier, C. J., Fantini, J., Barrantes, F. J. Disclosure of cholsterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor [en línea]. Scientific Reports. 2011. 1 (69). doi:10.1038/srep00069. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/1462Scientific Reports. 2011, 1 (69)reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaengspainfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:55:17Zoai:ucacris:123456789/1462instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:55:17.941Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse
dc.title.none.fl_str_mv Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
spellingShingle Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
Baier, Carlos J.
COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
title_short Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_full Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_fullStr Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_full_unstemmed Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_sort Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
dc.creator.none.fl_str_mv Baier, Carlos J.
Fantini, Jacques
Barrantes, Francisco José
author Baier, Carlos J.
author_facet Baier, Carlos J.
Fantini, Jacques
Barrantes, Francisco José
author_role author
author2 Fantini, Jacques
Barrantes, Francisco José
author2_role author
author
dc.subject.none.fl_str_mv COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
topic COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
dc.description.none.fl_txt_mv Fil: Baier, Carlos J. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Baier, Carlos J. Pontificia Universidad Católica Argentina. Programa de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentina
Fil: Baier, Carlos J. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Fantini, Jacques. Université Paul Cézanne; Francia
Fil: Fantini, Jacques. Université de la Méditerrané, Centre de Recherche en Neurobiologie et Neurophysiologie de Marseille; Francia
Fil: Barrantes, Francisco J. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Barrantes, Francisco J. Instituto de Investigaciones Bioquímicas de Bahíaa Blanca; Argentina
Fil: Barrantes, Francisco J. United Nations Educational, Scientific and Cultural Organization. Chair of Biophysics and Molecular Neurobiology; Francia
Abstract: Cholesterol influences ion-channel function, distribution and clustering in the membrane, endocytosis, and exocytic sorting of the nicotinic acetylcholine receptor (AChR). We report the occurrence of a cholesterol recognition motif, here coined ‘‘CARC’’, in the transmembrane regions of AChR subunits that bear extensive contact with the surrounding lipid, and are thus optimally suited to convey cholesterol-mediated signaling from the latter. Three cholesterol molecules could be docked on the transmembrane segments of each AChR subunit, rendering a total of 15 cholesterol molecules per AChR molecule. The CARC motifs contribute each with an energy of interaction between 35 and 52 kJ.mol21, adding up to a total of about 200 kJ.mol21 per receptor molecule, i.e. 40% of the lipid solvation free energy/ AChR molecule. The CARC motif is remarkably conserved along the phylogenetic scale, from prokaryotes to human, suggesting that it could be responsible for some of the above structural/functional properties of the AChR.
description Fil: Baier, Carlos J. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; Argentina
publishDate 2011
dc.date.none.fl_str_mv 2011
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 https://repositorio.uca.edu.ar/handle/123456789/1462
2045-2322
10.1038/srep00069
22355588
Baier, C. J., Fantini, J., Barrantes, F. J. Disclosure of cholsterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor [en línea]. Scientific Reports. 2011. 1 (69). doi:10.1038/srep00069. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/1462
url https://repositorio.uca.edu.ar/handle/123456789/1462
identifier_str_mv 2045-2322
10.1038/srep00069
22355588
Baier, C. J., Fantini, J., Barrantes, F. J. Disclosure of cholsterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor [en línea]. Scientific Reports. 2011. 1 (69). doi:10.1038/srep00069. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/1462
dc.language.none.fl_str_mv eng
spa
language eng
spa
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/4.0/
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Nature Research
publisher.none.fl_str_mv Nature Research
dc.source.none.fl_str_mv Scientific Reports. 2011, 1 (69)
reponame:Repositorio Institucional (UCA)
instname:Pontificia Universidad Católica Argentina
reponame_str Repositorio Institucional (UCA)
collection Repositorio Institucional (UCA)
instname_str Pontificia Universidad Católica Argentina
repository.name.fl_str_mv Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentina
repository.mail.fl_str_mv claudia_fernandez@uca.edu.ar
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score 13.22299

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