Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor

Abstract: Cholesterol influences ion-channel function, distribution and clustering in the membrane, endocytosis, and exocytic sorting of the nicotinic acetylcholine receptor (AChR). We report the occurrence of a cholesterol recognition motif, here coined ‘‘CARC’’, in the transmembrane regions of ACh...

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Detalles Bibliográficos
Autores principales: Baier, Carlos J., Fantini, Jacques, Barrantes, Francisco José
Formato: Artículo
Lenguaje:Inglés
Español
Publicado: Nature Research 2019
Materias:
COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/1462
Aporte de:
Repositorio Institucional de la Universidad Católica Argentina (UCA) de Universidad Católica Argentina
id I33-R139123456789-1462
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
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
spellingShingle COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
Baier, Carlos J.
Fantini, Jacques
Barrantes, Francisco José
Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
topic_facet COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
description Abstract: Cholesterol influences ion-channel function, distribution and clustering in the membrane, endocytosis, and exocytic sorting of the nicotinic acetylcholine receptor (AChR). We report the occurrence of a cholesterol recognition motif, here coined ‘‘CARC’’, in the transmembrane regions of AChR subunits that bear extensive contact with the surrounding lipid, and are thus optimally suited to convey cholesterol-mediated signaling from the latter. Three cholesterol molecules could be docked on the transmembrane segments of each AChR subunit, rendering a total of 15 cholesterol molecules per AChR molecule. The CARC motifs contribute each with an energy of interaction between 35 and 52 kJ.mol21, adding up to a total of about 200 kJ.mol21 per receptor molecule, i.e. 40% of the lipid solvation free energy/ AChR molecule. The CARC motif is remarkably conserved along the phylogenetic scale, from prokaryotes to human, suggesting that it could be responsible for some of the above structural/functional properties of the AChR.
format Artículo
author Baier, Carlos J.
Fantini, Jacques
Barrantes, Francisco José
author_facet Baier, Carlos J.
Fantini, Jacques
Barrantes, Francisco José
author_sort Baier, Carlos J.
title Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_short Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_full Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_fullStr Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_full_unstemmed Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_sort disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
publisher Nature Research
publishDate 2019
url https://repositorio.uca.edu.ar/handle/123456789/1462
work_keys_str_mv AT baiercarlosj disclosureofcholesterolrecognitionmotifsintransmembranedomainsofthehumannicotinicacetylcholinereceptor
AT fantinijacques disclosureofcholesterolrecognitionmotifsintransmembranedomainsofthehumannicotinicacetylcholinereceptor
AT barrantesfranciscojose disclosureofcholesterolrecognitionmotifsintransmembranedomainsofthehumannicotinicacetylcholinereceptor
bdutipo_str Repositorios
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