Transcriptional activation by AP‐2α is modulated by the oncogene DEK

Cell differentiation and development are highly regulated processes at the transcriptional level. One of the main transcription factors that regulate these processes is AP-2alpha, a cell-type specific protein required for vertebrate development and embryogenesis. AP-2alpha also regulates apoptosis a...

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Detalles Bibliográficos
Autores: Campillos, Mónica, García, Miguel Ángel, Valdivieso Amate, Fernando, Vázquez, Jesús
Tipo de recurso: artículo
Fecha de publicación:2003
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/8250
Acceso en línea:http://hdl.handle.net/10261/8250
Access Level:acceso abierto
Palabra clave:AP-2 in vitro
Oncoprotein DEK
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spelling Transcriptional activation by AP‐2α is modulated by the oncogene DEKCampillos, MónicaGarcía, Miguel ÁngelValdivieso Amate, FernandoVázquez, JesúsAP-2 in vitroOncoprotein DEKCell differentiation and development are highly regulated processes at the transcriptional level. One of the main transcription factors that regulate these processes is AP-2alpha, a cell-type specific protein required for vertebrate development and embryogenesis. AP-2alpha also regulates apoptosis and cell-cycle specific events by interacting with the oncogene c-Myc. In searching for novel AP-2alpha- interacting factors, using an affinity chromatography approach, we have observed that oncoprotein DEK interacts with AP-2alpha in vitro. The existence of an interaction between AP-2alpha and DEK in cellular cultures was demonstrated by expression of a tagged AP-2alpha form followed by immunodetection. By transient co-expression experiments using a reporter for APOE promoter activity we have found that DEK stimulates the transactivation activity of AP-2alpha over APOE promoter. Finally, electrophoretic mobility shift assays suggested that DEK enhances the DNA-binding activity of AP-2alpha. Our data suggest a novel cellular function of DEK as a transcriptional co-activatorThis work was supported by CICYT SAF 2000-0178 and 08.5/0065.1/2001 grants from Spanish Ministerio de Ciencia y Tecnología and from Comunidad Autónoma de Madrid, and by an institutional grant by Fundación Ramón Areces to CBMSOPeer reviewedOxford University PressMinisterio de Ciencia y Tecnología (España)Comunidad de MadridFundación Ramón Areces200820082003info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501122002 bytesapplication/pdfhttp://hdl.handle.net/10261/8250reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1093/nar/gkg247info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/82502026-05-22T06:33:51Z
dc.title.none.fl_str_mv Transcriptional activation by AP‐2α is modulated by the oncogene DEK
title Transcriptional activation by AP‐2α is modulated by the oncogene DEK
spellingShingle Transcriptional activation by AP‐2α is modulated by the oncogene DEK
Campillos, Mónica
AP-2 in vitro
Oncoprotein DEK
title_short Transcriptional activation by AP‐2α is modulated by the oncogene DEK
title_full Transcriptional activation by AP‐2α is modulated by the oncogene DEK
title_fullStr Transcriptional activation by AP‐2α is modulated by the oncogene DEK
title_full_unstemmed Transcriptional activation by AP‐2α is modulated by the oncogene DEK
title_sort Transcriptional activation by AP‐2α is modulated by the oncogene DEK
dc.creator.none.fl_str_mv Campillos, Mónica
García, Miguel Ángel
Valdivieso Amate, Fernando
Vázquez, Jesús
author Campillos, Mónica
author_facet Campillos, Mónica
García, Miguel Ángel
Valdivieso Amate, Fernando
Vázquez, Jesús
author_role author
author2 García, Miguel Ángel
Valdivieso Amate, Fernando
Vázquez, Jesús
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia y Tecnología (España)
Comunidad de Madrid
Fundación Ramón Areces
dc.subject.none.fl_str_mv AP-2 in vitro
Oncoprotein DEK
topic AP-2 in vitro
Oncoprotein DEK
description Cell differentiation and development are highly regulated processes at the transcriptional level. One of the main transcription factors that regulate these processes is AP-2alpha, a cell-type specific protein required for vertebrate development and embryogenesis. AP-2alpha also regulates apoptosis and cell-cycle specific events by interacting with the oncogene c-Myc. In searching for novel AP-2alpha- interacting factors, using an affinity chromatography approach, we have observed that oncoprotein DEK interacts with AP-2alpha in vitro. The existence of an interaction between AP-2alpha and DEK in cellular cultures was demonstrated by expression of a tagged AP-2alpha form followed by immunodetection. By transient co-expression experiments using a reporter for APOE promoter activity we have found that DEK stimulates the transactivation activity of AP-2alpha over APOE promoter. Finally, electrophoretic mobility shift assays suggested that DEK enhances the DNA-binding activity of AP-2alpha. Our data suggest a novel cellular function of DEK as a transcriptional co-activator
publishDate 2003
dc.date.none.fl_str_mv 2003
2008
2008
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/10261/8250
url http://hdl.handle.net/10261/8250
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1093/nar/gkg247
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 122002 bytes
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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
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repository.mail.fl_str_mv
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