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
- Institución
- Pontificia Universidad Católica Argentina
- OAI Identificador
- oai:ucacris:123456789/8736
Ver los metadatos del registro completo
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oai:ucacris:123456789/8736 |
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network_name_str |
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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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1836638347748966400 |
score |
13.22299 |