Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors

Abstract: Cholesterol is a ubiquitous neutral lipid, which finely tunes the activity of a wide range of membrane proteins, including neurotransmitter and hormone receptors and ion channels. Given the scarcity of available X-ray crystallographic structures and the even fewer in which cholesterol site...

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Detalles Bibliográficos
Autores principales: Di Scala, Coralie, Baier, Carlos J., Evans, Luke S., Williamson, Philip, T. F., Fantini, Jacques, Barrantes, Francisco José
Formato: Artículo
Lenguaje:Inglés
Español
Publicado: Elsevier 2019
Materias:
COLESTEROL
PROTEINAS
NEUROTRANSMISORES
Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/1460
Aporte de:
Repositorio Institucional de la Universidad Católica Argentina (UCA) de Universidad Católica Argentina
id I33-R139123456789-1460
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
Español
topic COLESTEROL
PROTEINAS
NEUROTRANSMISORES
spellingShingle COLESTEROL
PROTEINAS
NEUROTRANSMISORES
Di Scala, Coralie
Baier, Carlos J.
Evans, Luke S.
Williamson, Philip, T. F.
Fantini, Jacques
Barrantes, Francisco José
Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
topic_facet COLESTEROL
PROTEINAS
NEUROTRANSMISORES
description Abstract: Cholesterol is a ubiquitous neutral lipid, which finely tunes the activity of a wide range of membrane proteins, including neurotransmitter and hormone receptors and ion channels. Given the scarcity of available X-ray crystallographic structures and the even fewer in which cholesterol sites have been directly visualized, application of in silico computational methods remains a valid alternative for the detection and thermodynamic characterization of cholesterol-specific sites in functionally important membrane proteins. The membrane-embedded segments of the paradigm neurotransmitter receptor for acetylcholine display a series of cholesterol consensus domains (which we have coined “CARC”). The CARC motif exhibits a preference for the outer membrane leaflet and its mirror motif, CRAC, for the inner one. Some membrane proteins possess the double CARC–CRAC sequences within the same transmembrane domain. In addition to in silico molecular modeling, the affinity, concentration dependence, and specificity of the cholesterol-recognition motif–protein interaction have recently found experimental validation in other biophysical approaches like monolayer techniques and nuclear magnetic resonance spectroscopy. From the combined studies, it becomes apparent that the CARC motif is now more firmly established as a high-affinity cholesterol-binding domain for membrane-bound receptors and remarkably conserved along phylogenetic evolution.
format Artículo
author Di Scala, Coralie
Baier, Carlos J.
Evans, Luke S.
Williamson, Philip, T. F.
Fantini, Jacques
Barrantes, Francisco José
author_facet Di Scala, Coralie
Baier, Carlos J.
Evans, Luke S.
Williamson, Philip, T. F.
Fantini, Jacques
Barrantes, Francisco José
author_sort Di Scala, Coralie
title Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
title_short Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
title_full Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
title_fullStr Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
title_full_unstemmed Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
title_sort relevance of carc and crac cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
publisher Elsevier
publishDate 2019
url https://repositorio.uca.edu.ar/handle/123456789/1460
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