Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains

Abstract: We have previously shown that the intact nicotinic acetylcholine receptor (AChR) lacks preference for Lo domains when reconstituted in a sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model system (Bermúdez V, Antollini SS, Fernández-Nievas GA, Aveldaño MI, Barrantes FJ. J. Lipid...

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Autores principales: Perillo, Vanesa L., Peñalva, Daniel A., Vitale, Alejandro J., Barrantes, Francisco José, Antollini, Silvia S.
Formato: Artículo
Lenguaje:Inglés
Publicado: Elsevier 2022
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Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/15256
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id I33-R139-123456789-15256
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 PROTEINAS
FLUORESCENCIA
LIPIDOS
RECEPTORES NICOTINICOS
spellingShingle PROTEINAS
FLUORESCENCIA
LIPIDOS
RECEPTORES NICOTINICOS
Perillo, Vanesa L.
Peñalva, Daniel A.
Vitale, Alejandro J.
Barrantes, Francisco José
Antollini, Silvia S.
Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
topic_facet PROTEINAS
FLUORESCENCIA
LIPIDOS
RECEPTORES NICOTINICOS
description Abstract: We have previously shown that the intact nicotinic acetylcholine receptor (AChR) lacks preference for Lo domains when reconstituted in a sphingomyelin (SM), cholesterol (Chol) and POPC (1:1:1) model system (Bermúdez V, Antollini SS, Fernández-Nievas GA, Aveldaño MI, Barrantes FJ. J. Lipid Res. 2010; 51: 2629-2641). Here, we have furthered our studies by characterizing the influence of different lipid host compositions on the distribution of purified AChR reconstituted in two model systems (POPC:Chol, 1:1 and POPC:Chol:SM, 1:1:1), involving a) different SM species (porcine brain SM (bSM), 16:0-SM, 18:0-SM or 24:1-SM); or b) induced transbilayer asymmetry, resulting from enrichment in bSM in the external hemilayer. AChR distribution was evaluated by fluorescence resonance energy transfer efficiency between the AChR intrinsic fluorescence and Laurdan or dehydroergosterol fluorescence, and by analyzing the distribution of AChR in detergent-resistant and detergent-soluble fractions (1% Triton X-100, 4 °C). bSM-induced transbilayer asymmetry or the presence of 16:0-SM and/or 18:0-SM (unlike bSM or 24:1-SM) resulted in the preferential partitioning of AChR in Lo domains, suggesting that the localization of AChR in ordered domains strongly depends on the characteristics of the host lipid membrane, and in particular on the sphingolipid composition and transbilayer asymmetry.
format Artículo
author Perillo, Vanesa L.
Peñalva, Daniel A.
Vitale, Alejandro J.
Barrantes, Francisco José
Antollini, Silvia S.
author_facet Perillo, Vanesa L.
Peñalva, Daniel A.
Vitale, Alejandro J.
Barrantes, Francisco José
Antollini, Silvia S.
author_sort Perillo, Vanesa L.
title Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_short Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_full Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_fullStr Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_full_unstemmed Transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in Lo domains
title_sort transbilayer asymmetry and sphingomyelin composition modulate the preferential membrane partitioning of the nicotinic acetylcholine receptor in lo domains
publisher Elsevier
publishDate 2022
url https://repositorio.uca.edu.ar/handle/123456789/15256
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