Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels

Autores
Barrantes, Francisco José
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentina
Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: Using the crosstalk between the nicotinic acetylcholine receptor (nAChR) and its lipid microenvironment as a paradigm, this short overviewanalyzes the occurrence of structuralmotifswhich appear not only to be conserved within the nAChR family and contemporary eukaryotic members of the pentameric ligand-gated ion channel (pLGIC) superfamily, but also extend to prokaryotic homologues found in bacteria. The evolutionarily conserved design ismanifested in: 1) the concentric three-ring architecture of the transmembrane region, 2) the occurrence in this region of distinct lipid consensusmotifs in prokaryotic and eukaryotic pLGIC and 3) the key participation of the outer TM4 ring in conveying the influence of the lipidmembrane environment to themiddle TM1–TM3 ring and this, in turn, to the inner TM2 channel-lining ring, which determines the ion selectivity of the channel. The preservation of these constant structural–functional features throughout such a long phylogenetic span likely points to the successful gain-of-function conferred by their early acquisition. This article is part of a Special Issue entitled: Lipid–protein interactions.
Fuente
Biochimica et Biophysica Acta n° 1848, 2015
Materia
MEDICINA
RECEPTORES
PROTEINAS
LIPIDOS
CANALES IONICOS
COLESTEROL
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:123456789/8736

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oai_identifier_str oai:ucacris:123456789/8736
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
spelling Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channelsBarrantes, Francisco JoséMEDICINARECEPTORESPROTEINASLIPIDOSCANALES IONICOSCOLESTEROLFil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; ArgentinaFil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaAbstract: Using the crosstalk between the nicotinic acetylcholine receptor (nAChR) and its lipid microenvironment as a paradigm, this short overviewanalyzes the occurrence of structuralmotifswhich appear not only to be conserved within the nAChR family and contemporary eukaryotic members of the pentameric ligand-gated ion channel (pLGIC) superfamily, but also extend to prokaryotic homologues found in bacteria. The evolutionarily conserved design ismanifested in: 1) the concentric three-ring architecture of the transmembrane region, 2) the occurrence in this region of distinct lipid consensusmotifs in prokaryotic and eukaryotic pLGIC and 3) the key participation of the outer TM4 ring in conveying the influence of the lipidmembrane environment to themiddle TM1–TM3 ring and this, in turn, to the inner TM2 channel-lining ring, which determines the ion selectivity of the channel. The preservation of these constant structural–functional features throughout such a long phylogenetic span likely points to the successful gain-of-function conferred by their early acquisition. This article is part of a Special Issue entitled: Lipid–protein interactions.Elsevier B.V.2015info: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/123456789/87360006-300210.1016/j.bbamem.2015.03.028Barrantes FJ. Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels. Biochimica et Biophysica Acta. 2015; 1848. https://doi.org/10.1016/j.bbamem.2015.03.028. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8736Biochimica et Biophysica Acta n° 1848, 2015reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:56:54Zoai:ucacris:123456789/8736instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:56:55.148Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse
dc.title.none.fl_str_mv Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
title Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
spellingShingle Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
Barrantes, Francisco José
MEDICINA
RECEPTORES
PROTEINAS
LIPIDOS
CANALES IONICOS
COLESTEROL
title_short Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
title_full Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
title_fullStr Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
title_full_unstemmed Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
title_sort Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels
dc.creator.none.fl_str_mv Barrantes, Francisco José
author Barrantes, Francisco José
author_facet Barrantes, Francisco José
author_role author
dc.subject.none.fl_str_mv MEDICINA
RECEPTORES
PROTEINAS
LIPIDOS
CANALES IONICOS
COLESTEROL
topic MEDICINA
RECEPTORES
PROTEINAS
LIPIDOS
CANALES IONICOS
COLESTEROL
dc.description.none.fl_txt_mv Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentina
Fil: Barrantes, Francisco José. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Abstract: Using the crosstalk between the nicotinic acetylcholine receptor (nAChR) and its lipid microenvironment as a paradigm, this short overviewanalyzes the occurrence of structuralmotifswhich appear not only to be conserved within the nAChR family and contemporary eukaryotic members of the pentameric ligand-gated ion channel (pLGIC) superfamily, but also extend to prokaryotic homologues found in bacteria. The evolutionarily conserved design ismanifested in: 1) the concentric three-ring architecture of the transmembrane region, 2) the occurrence in this region of distinct lipid consensusmotifs in prokaryotic and eukaryotic pLGIC and 3) the key participation of the outer TM4 ring in conveying the influence of the lipidmembrane environment to themiddle TM1–TM3 ring and this, in turn, to the inner TM2 channel-lining ring, which determines the ion selectivity of the channel. The preservation of these constant structural–functional features throughout such a long phylogenetic span likely points to the successful gain-of-function conferred by their early acquisition. This article is part of a Special Issue entitled: Lipid–protein interactions.
description Fil: Barrantes, Francisco José. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentina
publishDate 2015
dc.date.none.fl_str_mv 2015
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/123456789/8736
0006-3002
10.1016/j.bbamem.2015.03.028
Barrantes FJ. Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels. Biochimica et Biophysica Acta. 2015; 1848. https://doi.org/10.1016/j.bbamem.2015.03.028. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8736
url https://repositorio.uca.edu.ar/handle/123456789/8736
identifier_str_mv 0006-3002
10.1016/j.bbamem.2015.03.028
Barrantes FJ. Phylogenetic conservation of protein–lipid motifs in pentameric ligand-gated ion channels. Biochimica et Biophysica Acta. 2015; 1848. https://doi.org/10.1016/j.bbamem.2015.03.028. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8736
dc.language.none.fl_str_mv eng
language eng
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 Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv Biochimica et Biophysica Acta n° 1848, 2015
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