Phylogenetic conservation of protein-lipid motifs in pentameric ligand-gated ion channels
- Autores
- Barrantes, Francisco Jose
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Using the crosstalk between the nicotinic acetylcholine receptor (nAChR) and its lipid microenvironment as a paradigm, this short overview analyzes the occurrence of structural motifs which 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 is manifested in: 1) the concentric three-ring architecture of the transmembrane region, 2) the occurrence in this region of distinct lipid consensus motifs in prokaryotic and eukaryotic pLGIC and 3) the key participation of the outer TM4 ring in conveying the influence of the lipid membrane environment to the middle 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.
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Instituto de Investigaciones Biomédicas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas; Argentina - Materia
-
ACETYLCHOLINE RECEPTOR
BACTERIAL HOMOLOGUES
BACTERIAL ION CHANNELS
CHOLESTEROL
LIPID-PROTEIN INTERACTIONS
PENTAMERIC LIGAND-GATED ION CHANNELS
SYNAPTIC RECEPTORS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/38364
Ver los metadatos del registro completo
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spelling |
Phylogenetic conservation of protein-lipid motifs in pentameric ligand-gated ion channelsBarrantes, Francisco JoseACETYLCHOLINE RECEPTORBACTERIAL HOMOLOGUESBACTERIAL ION CHANNELSCHOLESTEROLLIPID-PROTEIN INTERACTIONSPENTAMERIC LIGAND-GATED ION CHANNELSSYNAPTIC RECEPTORShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Using the crosstalk between the nicotinic acetylcholine receptor (nAChR) and its lipid microenvironment as a paradigm, this short overview analyzes the occurrence of structural motifs which 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 is manifested in: 1) the concentric three-ring architecture of the transmembrane region, 2) the occurrence in this region of distinct lipid consensus motifs in prokaryotic and eukaryotic pLGIC and 3) the key participation of the outer TM4 ring in conveying the influence of the lipid membrane environment to the middle 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.Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Instituto de Investigaciones Biomédicas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas; ArgentinaElsevier Science2015-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/38364Barrantes, Francisco Jose; Phylogenetic conservation of protein-lipid motifs in pentameric ligand-gated ion channels; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1848; 9; 7-2015; 1796-18050005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2015.03.028info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273615001078info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:12:04Zoai:ri.conicet.gov.ar:11336/38364instacron: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 10:12:05.232CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
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 Jose ACETYLCHOLINE RECEPTOR BACTERIAL HOMOLOGUES BACTERIAL ION CHANNELS CHOLESTEROL LIPID-PROTEIN INTERACTIONS PENTAMERIC LIGAND-GATED ION CHANNELS SYNAPTIC RECEPTORS |
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 Jose |
author |
Barrantes, Francisco Jose |
author_facet |
Barrantes, Francisco Jose |
author_role |
author |
dc.subject.none.fl_str_mv |
ACETYLCHOLINE RECEPTOR BACTERIAL HOMOLOGUES BACTERIAL ION CHANNELS CHOLESTEROL LIPID-PROTEIN INTERACTIONS PENTAMERIC LIGAND-GATED ION CHANNELS SYNAPTIC RECEPTORS |
topic |
ACETYLCHOLINE RECEPTOR BACTERIAL HOMOLOGUES BACTERIAL ION CHANNELS CHOLESTEROL LIPID-PROTEIN INTERACTIONS PENTAMERIC LIGAND-GATED ION CHANNELS SYNAPTIC RECEPTORS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Using the crosstalk between the nicotinic acetylcholine receptor (nAChR) and its lipid microenvironment as a paradigm, this short overview analyzes the occurrence of structural motifs which 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 is manifested in: 1) the concentric three-ring architecture of the transmembrane region, 2) the occurrence in this region of distinct lipid consensus motifs in prokaryotic and eukaryotic pLGIC and 3) the key participation of the outer TM4 ring in conveying the influence of the lipid membrane environment to the middle 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. Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Instituto de Investigaciones Biomédicas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas; Argentina |
description |
Using the crosstalk between the nicotinic acetylcholine receptor (nAChR) and its lipid microenvironment as a paradigm, this short overview analyzes the occurrence of structural motifs which 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 is manifested in: 1) the concentric three-ring architecture of the transmembrane region, 2) the occurrence in this region of distinct lipid consensus motifs in prokaryotic and eukaryotic pLGIC and 3) the key participation of the outer TM4 ring in conveying the influence of the lipid membrane environment to the middle 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. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-07 |
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/11336/38364 Barrantes, Francisco Jose; Phylogenetic conservation of protein-lipid motifs in pentameric ligand-gated ion channels; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1848; 9; 7-2015; 1796-1805 0005-2736 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/38364 |
identifier_str_mv |
Barrantes, Francisco Jose; Phylogenetic conservation of protein-lipid motifs in pentameric ligand-gated ion channels; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1848; 9; 7-2015; 1796-1805 0005-2736 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2015.03.028 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273615001078 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
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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1842270184372436992 |
score |
13.13397 |