Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains

Autores
Fantini, Jacques; Di Scala, Coralie; Baier, Carlos J.; Barrantes, Francisco José
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión aceptada
Descripción
Fil: Fantini, Jacques. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Francia
Fil: Di Scala, Coralie. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Francia
Fil: Baier, Carlos J. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentina
Fil: Baier, Carlos J. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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: The molecular mechanisms that control the multiple possible modes of protein association with membrane cholesterol are remarkably convergent. These mechanisms, which include hydrogen bonding, CH-π stacking and dispersion forces, are used by a wide variety of extracellular proteins (e.g. microbial or amyloid) and membrane receptors. Virus fusion peptides penetrate the membrane of host cells with a tilted orientation that is compatible with a transient interaction with cholesterol; this tilted orientation is also characteristic of the process of insertion of amyloid proteins that subsequently form oligomeric pores in the plasma membrane of brain cells. Membrane receptors that are associated with cholesterol generally display linear consensus binding motifs (CARC and CRAC) characterized by a triad of basic (Lys/Arg), aromatic (Tyr/phe) and aliphatic (Leu/Val) amino acid residues. In some cases, the presence of both CARC and CRAC within the same membrane-spanning domain allows the simultaneous binding of two cholesterol molecules, one in each membrane leaflet. In this review the molecular basis and the functional significance of the different modes of protein-cholesterol interactions in plasma membranes are discussed.
Fuente
Chemistry and Physics of Lipids. 2016;199:52-60
Materia
AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
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:123456789/8789
Acceder
id RIUCA_ea7d59e65b83a3e02606060df7736590
oai_identifier_str oai:ucacris:123456789/8789
network_acronym_str RIUCA
repository_id_str 2585
network_name_str Repositorio Institucional (UCA)
spelling Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domainsFantini, JacquesDi Scala, CoralieBaier, Carlos J.Barrantes, Francisco JoséAMINOACIDOSCOLESTEROLLIPIDOSPROTEINASMEMBRANA CELULARFil: Fantini, Jacques. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; FranciaFil: Di Scala, Coralie. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; FranciaFil: Baier, Carlos J. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; ArgentinaFil: Baier, Carlos J. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: 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: The molecular mechanisms that control the multiple possible modes of protein association with membrane cholesterol are remarkably convergent. These mechanisms, which include hydrogen bonding, CH-π stacking and dispersion forces, are used by a wide variety of extracellular proteins (e.g. microbial or amyloid) and membrane receptors. Virus fusion peptides penetrate the membrane of host cells with a tilted orientation that is compatible with a transient interaction with cholesterol; this tilted orientation is also characteristic of the process of insertion of amyloid proteins that subsequently form oligomeric pores in the plasma membrane of brain cells. Membrane receptors that are associated with cholesterol generally display linear consensus binding motifs (CARC and CRAC) characterized by a triad of basic (Lys/Arg), aromatic (Tyr/phe) and aliphatic (Leu/Val) amino acid residues. In some cases, the presence of both CARC and CRAC within the same membrane-spanning domain allows the simultaneous binding of two cholesterol molecules, one in each membrane leaflet. In this review the molecular basis and the functional significance of the different modes of protein-cholesterol interactions in plasma membranes are discussed.Elsevier2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://repositorio.uca.edu.ar/handle/123456789/87890009-3084 (impreso)1873-2941 (online)10.1016/j.chemphyslip.2016.02.00926987951Fantini J, Di Scala C, Baier CJ, Barrantes FJ. Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains [en línea]. Chemistry and Physics of Lipids. 2016;199:52-60. doi:10.1016/j.chemphyslip.2016.02.009 Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8789Chemistry and Physics of Lipids. 2016;199:52-60reponame:Repositorio Institucional (UCA)instname:Pontificia Universidad Católica Argentinaenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/4.0/2025-07-03T10:56:56Zoai:ucacris:123456789/8789instacron:UCAInstitucionalhttps://repositorio.uca.edu.ar/Universidad privadaNo correspondehttps://repositorio.uca.edu.ar/oaiclaudia_fernandez@uca.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:25852025-07-03 10:56:57.061Repositorio Institucional (UCA) - Pontificia Universidad Católica Argentinafalse
dc.title.none.fl_str_mv Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
title Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
spellingShingle Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
Fantini, Jacques
AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
title_short Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
title_full Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
title_fullStr Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
title_full_unstemmed Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
title_sort Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
dc.creator.none.fl_str_mv Fantini, Jacques
Di Scala, Coralie
Baier, Carlos J.
Barrantes, Francisco José
author Fantini, Jacques
author_facet Fantini, Jacques
Di Scala, Coralie
Baier, Carlos J.
Barrantes, Francisco José
author_role author
author2 Di Scala, Coralie
Baier, Carlos J.
Barrantes, Francisco José
author2_role author
author
author
dc.subject.none.fl_str_mv AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
topic AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
dc.description.none.fl_txt_mv Fil: Fantini, Jacques. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Francia
Fil: Di Scala, Coralie. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Francia
Fil: Baier, Carlos J. Pontificia Universidad Católica Argentina. Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas. Laboratorio de Neurobiología Molecular; Argentina
Fil: Baier, Carlos J. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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: The molecular mechanisms that control the multiple possible modes of protein association with membrane cholesterol are remarkably convergent. These mechanisms, which include hydrogen bonding, CH-π stacking and dispersion forces, are used by a wide variety of extracellular proteins (e.g. microbial or amyloid) and membrane receptors. Virus fusion peptides penetrate the membrane of host cells with a tilted orientation that is compatible with a transient interaction with cholesterol; this tilted orientation is also characteristic of the process of insertion of amyloid proteins that subsequently form oligomeric pores in the plasma membrane of brain cells. Membrane receptors that are associated with cholesterol generally display linear consensus binding motifs (CARC and CRAC) characterized by a triad of basic (Lys/Arg), aromatic (Tyr/phe) and aliphatic (Leu/Val) amino acid residues. In some cases, the presence of both CARC and CRAC within the same membrane-spanning domain allows the simultaneous binding of two cholesterol molecules, one in each membrane leaflet. In this review the molecular basis and the functional significance of the different modes of protein-cholesterol interactions in plasma membranes are discussed.
description Fil: Fantini, Jacques. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Francia
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://repositorio.uca.edu.ar/handle/123456789/8789
0009-3084 (impreso)
1873-2941 (online)
10.1016/j.chemphyslip.2016.02.009
26987951
Fantini J, Di Scala C, Baier CJ, Barrantes FJ. Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains [en línea]. Chemistry and Physics of Lipids. 2016;199:52-60. doi:10.1016/j.chemphyslip.2016.02.009 Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8789
url https://repositorio.uca.edu.ar/handle/123456789/8789
identifier_str_mv 0009-3084 (impreso)
1873-2941 (online)
10.1016/j.chemphyslip.2016.02.009
26987951
Fantini J, Di Scala C, Baier CJ, Barrantes FJ. Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains [en línea]. Chemistry and Physics of Lipids. 2016;199:52-60. doi:10.1016/j.chemphyslip.2016.02.009 Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8789
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
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Chemistry and Physics of Lipids. 2016;199:52-60
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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