Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9

© 2015 Elsevier B.V. The tetraspanin CD9 has been shown to interact with different members of the β1 and β3 subfamilies of integrins, regulating through these interactions cell adhesion, migration and signaling. Based on confocal microscopy co-localization and on co-immunoprecipitation results, we r...

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Detalles Bibliográficos
Autores: Reyes, Raquel, Monjas, Alicia, Cardeñes, Beatriz, Gilsanz, Álvaro, Machado-Pineda, Yesenia, Cabañas, Carlos
Tipo de recurso: artículo
Estado:Versión publicada
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:10261/133553
Acceso en línea:http://hdl.handle.net/10261/133553
Access Level:acceso abierto
Palabra clave:CD9
Tetraspanin
Adhesion
Cytotoxicity
LFA-1
Integrin
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spelling Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9Reyes, RaquelMonjas, AliciaCardeñes, BeatrizGilsanz, ÁlvaroMachado-Pineda, YeseniaCabañas, CarlosCD9TetraspaninAdhesionCytotoxicityLFA-1Integrin© 2015 Elsevier B.V. The tetraspanin CD9 has been shown to interact with different members of the β1 and β3 subfamilies of integrins, regulating through these interactions cell adhesion, migration and signaling. Based on confocal microscopy co-localization and on co-immunoprecipitation results, we report here that CD9 associates with the β2 integrin LFA-1 in different types of leukocytes including T, B and monocytic cells. This association is resistant to stringent solubilization conditions which, together with data from chemical crosslinking, in situ Proximity Ligation Assays and pull-down experiments, suggest a primary/direct type of interaction mediated by the Large Extracellular Loop of the tetraspanin. CD9 exerts inhibitory effects on the adhesive function of LFA-1 and on LFA-1-dependent leukocyte cytotoxic activity. The mechanism responsible for this negative regulation exerted by CD9 on LFA-1 adhesion does not involve changes in the affinity state of this integrin but seems to be related to alterations in its state of aggregation.SAF2012-34561 from the Spanish «Ministerio de Economía y Competitividad-MINECOPeer ReviewedMinisterio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2016201620152016info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/133553reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1335532026-05-22T06:33:51Z
dc.title.none.fl_str_mv Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
title Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
spellingShingle Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
Reyes, Raquel
CD9
Tetraspanin
Adhesion
Cytotoxicity
LFA-1
Integrin
title_short Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
title_full Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
title_fullStr Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
title_full_unstemmed Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
title_sort Different states of integrin LFA-1 aggregation are controlled through its association with tetraspanin CD9
dc.creator.none.fl_str_mv Reyes, Raquel
Monjas, Alicia
Cardeñes, Beatriz
Gilsanz, Álvaro
Machado-Pineda, Yesenia
Cabañas, Carlos
author Reyes, Raquel
author_facet Reyes, Raquel
Monjas, Alicia
Cardeñes, Beatriz
Gilsanz, Álvaro
Machado-Pineda, Yesenia
Cabañas, Carlos
author_role author
author2 Monjas, Alicia
Cardeñes, Beatriz
Gilsanz, Álvaro
Machado-Pineda, Yesenia
Cabañas, Carlos
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv CD9
Tetraspanin
Adhesion
Cytotoxicity
LFA-1
Integrin
topic CD9
Tetraspanin
Adhesion
Cytotoxicity
LFA-1
Integrin
description © 2015 Elsevier B.V. The tetraspanin CD9 has been shown to interact with different members of the β1 and β3 subfamilies of integrins, regulating through these interactions cell adhesion, migration and signaling. Based on confocal microscopy co-localization and on co-immunoprecipitation results, we report here that CD9 associates with the β2 integrin LFA-1 in different types of leukocytes including T, B and monocytic cells. This association is resistant to stringent solubilization conditions which, together with data from chemical crosslinking, in situ Proximity Ligation Assays and pull-down experiments, suggest a primary/direct type of interaction mediated by the Large Extracellular Loop of the tetraspanin. CD9 exerts inhibitory effects on the adhesive function of LFA-1 and on LFA-1-dependent leukocyte cytotoxic activity. The mechanism responsible for this negative regulation exerted by CD9 on LFA-1 adhesion does not involve changes in the affinity state of this integrin but seems to be related to alterations in its state of aggregation.
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
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/133553
url http://hdl.handle.net/10261/133553
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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 15,81155

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