Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6

The Wnt canonical ligands elicit the activation of β-catenin transcriptional activity, a response dependent on, but not limited to, β-catenin stabilization through the inhibition of GSK3 activity. Two mechanisms have been proposed for this inhibition, one dependent on the binding and subsequent bloc...

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Autores: Vinyoles, Meritxell, Valle Pérez, Beatriz del, Curto, Josué, Viñas Castells, Rosa, 1985-, Alba Castellón, Lorena, 1984-, García de Herreros, Antonio, Duñach, Mireia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10230/23820
Acceso en línea:http://hdl.handle.net/10230/23820
http://dx.doi.org/10.1016/j.molcel.2013.12.010
Access Level:acceso abierto
Palabra clave:Fosforilació
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spelling Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6Vinyoles, MeritxellValle Pérez, Beatriz delCurto, JosuéViñas Castells, Rosa, 1985-Alba Castellón, Lorena, 1984-García de Herreros, AntonioDuñach, MireiaFosforilacióThe Wnt canonical ligands elicit the activation of β-catenin transcriptional activity, a response dependent on, but not limited to, β-catenin stabilization through the inhibition of GSK3 activity. Two mechanisms have been proposed for this inhibition, one dependent on the binding and subsequent block of GSK3 to LRP5/6 Wnt coreceptor and another one on its sequestration into multivesicular bodies (MVBs). Here we report that internalization of the GSK3-containing Wnt-signalosome complex into MVBs is dependent on the dissociation of p120-catenin/cadherin from this complex. Disruption of cadherin-LRP5/6 interaction is controlled by cadherin phosphorylation and requires the previous separation of p120-catenin; thus, p120-catenin and cadherin mutants unable to dissociate from the complex block GSK3 sequestration into MVBs. These mutants substantially inhibit, but do not completely prevent, the β-catenin upregulation caused by Wnt3a. These results, besides elucidating how GSK3 is sequestered into MVBs, support this mechanism as cause of β-catenin stabilization by Wnt.This work was funded by grants from the Ministerio de Economía (BFU2012-31554 to M.D. and SAF2010-16089 to A.G.H.) and Fundació La Marató de TV3 (120130) to M.D. and A.G.H. Support from Fundación Científica de la Asociación Española contra el Cáncer, ISCIII/FEDER (RD12/0036/005) and Generalitat de Catalunya (2009SGR867) is also appreciated. M.V. and L.A.-C. were recipients of predoctoral fellowships from FPI, and R.V.-C. was a recipient of a fellowship from ISCIIIElsevier201520152014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/23820http://dx.doi.org/10.1016/j.molcel.2013.12.010reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésMolecular cell. 2014;53(3):444-57info:eu-repo/grantAgreement/ES/3PN/BFU2012-31554info:eu-repo/grantAgreement/ES/3PN/SAF2010-16089© Elsevier This is the published version of an article http://dx.doi.org/10.1016/j.molcel.2013.12.010 that appeared in the journal Molecular cell. It is published in an Open Archive under an Elsevier user license. Details of this licence are available here: http://www.elsevier.com/about/open-access/open-access-policies/oa-license-policy/elsevier-user-licenseinfo:eu-repo/semantics/openAccessoai:recercat.cat:10230/238202026-05-29T05:05:01Z
dc.title.none.fl_str_mv Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
title Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
spellingShingle Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
Vinyoles, Meritxell
Fosforilació
title_short Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
title_full Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
title_fullStr Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
title_full_unstemmed Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
title_sort Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6
dc.creator.none.fl_str_mv Vinyoles, Meritxell
Valle Pérez, Beatriz del
Curto, Josué
Viñas Castells, Rosa, 1985-
Alba Castellón, Lorena, 1984-
García de Herreros, Antonio
Duñach, Mireia
author Vinyoles, Meritxell
author_facet Vinyoles, Meritxell
Valle Pérez, Beatriz del
Curto, Josué
Viñas Castells, Rosa, 1985-
Alba Castellón, Lorena, 1984-
García de Herreros, Antonio
Duñach, Mireia
author_role author
author2 Valle Pérez, Beatriz del
Curto, Josué
Viñas Castells, Rosa, 1985-
Alba Castellón, Lorena, 1984-
García de Herreros, Antonio
Duñach, Mireia
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Fosforilació
topic Fosforilació
description The Wnt canonical ligands elicit the activation of β-catenin transcriptional activity, a response dependent on, but not limited to, β-catenin stabilization through the inhibition of GSK3 activity. Two mechanisms have been proposed for this inhibition, one dependent on the binding and subsequent block of GSK3 to LRP5/6 Wnt coreceptor and another one on its sequestration into multivesicular bodies (MVBs). Here we report that internalization of the GSK3-containing Wnt-signalosome complex into MVBs is dependent on the dissociation of p120-catenin/cadherin from this complex. Disruption of cadherin-LRP5/6 interaction is controlled by cadherin phosphorylation and requires the previous separation of p120-catenin; thus, p120-catenin and cadherin mutants unable to dissociate from the complex block GSK3 sequestration into MVBs. These mutants substantially inhibit, but do not completely prevent, the β-catenin upregulation caused by Wnt3a. These results, besides elucidating how GSK3 is sequestered into MVBs, support this mechanism as cause of β-catenin stabilization by Wnt.
publishDate 2014
dc.date.none.fl_str_mv 2014
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/23820
http://dx.doi.org/10.1016/j.molcel.2013.12.010
url http://hdl.handle.net/10230/23820
http://dx.doi.org/10.1016/j.molcel.2013.12.010
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Molecular cell. 2014;53(3):444-57
info:eu-repo/grantAgreement/ES/3PN/BFU2012-31554
info:eu-repo/grantAgreement/ES/3PN/SAF2010-16089
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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