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

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. mi...

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Detalles Bibliográficos
Autores principales: Fantini, Jacques, Di Scala, Coralie, Baier, Carlos J., Barrantes, Francisco José
Formato: Artículo
Lenguaje:Inglés
Publicado: Elsevier 2019
Materias:
AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/8789
Aporte de:
Repositorio Institucional de la Universidad Católica Argentina (UCA) de Universidad Católica Argentina
id I33-R139123456789-8789
record_format dspace
institution Universidad Católica Argentina
institution_str I-33
repository_str R-139
collection Repositorio Institucional de la Universidad Católica Argentina (UCA)
language Inglés
topic AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
spellingShingle AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
Fantini, Jacques
Di Scala, Coralie
Baier, Carlos J.
Barrantes, Francisco José
Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
topic_facet AMINOACIDOS
COLESTEROL
LIPIDOS
PROTEINAS
MEMBRANA CELULAR
description 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.
format Artículo
author Fantini, Jacques
Di Scala, Coralie
Baier, Carlos J.
Barrantes, Francisco José
author_facet Fantini, Jacques
Di Scala, Coralie
Baier, Carlos J.
Barrantes, Francisco José
author_sort Fantini, Jacques
title Molecular mechanisms of protein-cholesterol interactions in plasma membranes : functional distinction between topological (tilted) and consensus (CARC/CRAC) domains
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
publisher Elsevier
publishDate 2019
url https://repositorio.uca.edu.ar/handle/123456789/8789
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