Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains

© 2014 Elsevier B.V. In the last decade an increasing number of plasma membrane (PM) proteins have been shown to be non-randomly distributed but instead forming submicron-sized oligomers called nanoclusters. Nanoclusters exist independently of the ligand-bound state of the receptors and their existe...

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Autores: Beck-García, Katharina, Beck-García, Esmeralda, Bohler, Sheila, Zorzin, Carina, Sezgin, Erdinc, Levantal, Ilya, Alarcón, Balbino, Schamel, Wolfgang
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/139941
Acceso en línea:http://hdl.handle.net/10261/139941
Access Level:acceso abierto
Palabra clave:Lipid
Cholesterol
Membrane
Nanoclustering
TCR
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spelling Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domainsBeck-García, KatharinaBeck-García, EsmeraldaBohler, SheilaZorzin, CarinaSezgin, ErdincLevantal, IlyaAlarcón, BalbinoSchamel, WolfgangLipidCholesterolMembraneNanoclusteringTCR© 2014 Elsevier B.V. In the last decade an increasing number of plasma membrane (PM) proteins have been shown to be non-randomly distributed but instead forming submicron-sized oligomers called nanoclusters. Nanoclusters exist independently of the ligand-bound state of the receptors and their existence implies a high degree of lateral organisation of the PM and its proteins. The mechanisms that drive receptor nanoclustering are largely unknown. One well-defined example of a transmembrane receptor that forms nanoclusters is the T cell antigen receptor (TCR), a multisubunit protein complex whose nanoclustering influences its activity. Membrane lipids, namely cholesterol and sphingomyelin, have been shown to contribute to TCR nanoclustering. However, the identity of the membrane microdomain in which the TCR resides remains controversial. Using a GFP-labeled TCR we show here that the resting TCR localized in the disordered domain of giant PM vesicles (GPMVs) and PM spheres (PMSs) and that single and nanoclustered TCRs are found in the high-density fractions in sucrose gradients. Both findings are indicative of non-raft localization. We discuss possible mechanisms of TCR nanoclustering in T cells. This article is part of a Special Issue entitled: Nanoscale membrane organisation and signalling.German Research Foundation (GSC-4, the Spemann Graduate School and EXC294, the BIOSS Center for Biological Signalling Studies, by the German Research Foundation grant SCH 976/2-1, and by the European Union through grant FP7/2007-2013 SYBILLAPeer ReviewedElsevierGerman Research FoundationEuropean Commission2016201620152016info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/139941reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglésinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1399412026-05-22T06:33:51Z
dc.title.none.fl_str_mv Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
title Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
spellingShingle Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
Beck-García, Katharina
Lipid
Cholesterol
Membrane
Nanoclustering
TCR
title_short Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
title_full Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
title_fullStr Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
title_full_unstemmed Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
title_sort Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains
dc.creator.none.fl_str_mv Beck-García, Katharina
Beck-García, Esmeralda
Bohler, Sheila
Zorzin, Carina
Sezgin, Erdinc
Levantal, Ilya
Alarcón, Balbino
Schamel, Wolfgang
author Beck-García, Katharina
author_facet Beck-García, Katharina
Beck-García, Esmeralda
Bohler, Sheila
Zorzin, Carina
Sezgin, Erdinc
Levantal, Ilya
Alarcón, Balbino
Schamel, Wolfgang
author_role author
author2 Beck-García, Esmeralda
Bohler, Sheila
Zorzin, Carina
Sezgin, Erdinc
Levantal, Ilya
Alarcón, Balbino
Schamel, Wolfgang
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv German Research Foundation
European Commission
dc.subject.none.fl_str_mv Lipid
Cholesterol
Membrane
Nanoclustering
TCR
topic Lipid
Cholesterol
Membrane
Nanoclustering
TCR
description © 2014 Elsevier B.V. In the last decade an increasing number of plasma membrane (PM) proteins have been shown to be non-randomly distributed but instead forming submicron-sized oligomers called nanoclusters. Nanoclusters exist independently of the ligand-bound state of the receptors and their existence implies a high degree of lateral organisation of the PM and its proteins. The mechanisms that drive receptor nanoclustering are largely unknown. One well-defined example of a transmembrane receptor that forms nanoclusters is the T cell antigen receptor (TCR), a multisubunit protein complex whose nanoclustering influences its activity. Membrane lipids, namely cholesterol and sphingomyelin, have been shown to contribute to TCR nanoclustering. However, the identity of the membrane microdomain in which the TCR resides remains controversial. Using a GFP-labeled TCR we show here that the resting TCR localized in the disordered domain of giant PM vesicles (GPMVs) and PM spheres (PMSs) and that single and nanoclustered TCRs are found in the high-density fractions in sucrose gradients. Both findings are indicative of non-raft localization. We discuss possible mechanisms of TCR nanoclustering in T cells. This article is part of a Special Issue entitled: Nanoscale membrane organisation and signalling.
publishDate 2015
dc.date.none.fl_str_mv 2015
2016
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/139941
url http://hdl.handle.net/10261/139941
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.811543

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