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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/38364

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oai_identifier_str oai:ri.conicet.gov.ar:11336/38364
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
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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