The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators

Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins regulates many processes in the eukaryotic cell. This reaction is similar to ubiquitination and usually requires an E3 ligase for substrate modification. However, only a few SUMO ligases have been described so far, which frequen...

Descripción completa

Detalles Bibliográficos
Autores: García-Gutiérrez, Pablo, Juárez-Vicente, Francisco, Gallardo-Chamizo, Francisco, Charnay, Patrick, García-Domínguez, Mario
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2011
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/52347
Acceso en línea:http://hdl.handle.net/10261/52347
Access Level:acceso abierto
Palabra clave:Krox20
Nab
SUMO ligase
Ubc9
id ES_6f089f887675d7e8a384dc9669d94f2f
oai_identifier_str oai:digital.csic.es:10261/52347
network_acronym_str ES
network_name_str España
repository_id_str
spelling The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulatorsGarcía-Gutiérrez, PabloJuárez-Vicente, FranciscoGallardo-Chamizo, FranciscoCharnay, PatrickGarcía-Domínguez, MarioKrox20NabSUMO ligaseUbc9Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins regulates many processes in the eukaryotic cell. This reaction is similar to ubiquitination and usually requires an E3 ligase for substrate modification. However, only a few SUMO ligases have been described so far, which frequently facilitate sumoylation by bringing together the SUMO-conjugating enzyme Ubc9 and the target protein. Ubc9 is an interaction partner of the transcription factor Krox20, a key regulator of hindbrain development. Here, we show that Krox20 functions as a SUMO ligase for its coregulators-the Nab proteins-and that Nab sumoylation negatively modulates Krox20 transcriptional activity in vivo. © 2011 EuropeEan MoleEcular Biology Oorganization.This work was supported by BFU2009-10986/BMC (MICINN) and Intramural 200920I085 (CSIC) grants.Peer ReviewedNature Publishing GroupMinisterio de Ciencia e Innovación (España)Consejo Superior de Investigaciones Científicas (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2012201220112012info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Preprintinfo:eu-repo/semantics/submittedVersionhttp://hdl.handle.net/10261/52347reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1038/embor.2011.152Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/523472026-05-22T06:33:51Z
dc.title.none.fl_str_mv The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
title The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
spellingShingle The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
García-Gutiérrez, Pablo
Krox20
Nab
SUMO ligase
Ubc9
title_short The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
title_full The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
title_fullStr The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
title_full_unstemmed The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
title_sort The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
dc.creator.none.fl_str_mv García-Gutiérrez, Pablo
Juárez-Vicente, Francisco
Gallardo-Chamizo, Francisco
Charnay, Patrick
García-Domínguez, Mario
author García-Gutiérrez, Pablo
author_facet García-Gutiérrez, Pablo
Juárez-Vicente, Francisco
Gallardo-Chamizo, Francisco
Charnay, Patrick
García-Domínguez, Mario
author_role author
author2 Juárez-Vicente, Francisco
Gallardo-Chamizo, Francisco
Charnay, Patrick
García-Domínguez, Mario
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
Consejo Superior de Investigaciones Científicas (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Krox20
Nab
SUMO ligase
Ubc9
topic Krox20
Nab
SUMO ligase
Ubc9
description Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins regulates many processes in the eukaryotic cell. This reaction is similar to ubiquitination and usually requires an E3 ligase for substrate modification. However, only a few SUMO ligases have been described so far, which frequently facilitate sumoylation by bringing together the SUMO-conjugating enzyme Ubc9 and the target protein. Ubc9 is an interaction partner of the transcription factor Krox20, a key regulator of hindbrain development. Here, we show that Krox20 functions as a SUMO ligase for its coregulators-the Nab proteins-and that Nab sumoylation negatively modulates Krox20 transcriptional activity in vivo. © 2011 EuropeEan MoleEcular Biology Oorganization.
publishDate 2011
dc.date.none.fl_str_mv 2011
2012
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Preprint
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/52347
url http://hdl.handle.net/10261/52347
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1038/embor.2011.152
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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
_version_ 1869410466808201216
score 15,812429

Similares en LA Referencia