Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein

To effectively direct targeted repression, the class I histone deacetylases (HDACs) associate with many important regulatory proteins. In this paper we describe the molecular characterization of a member of the Jumonji domain 2 (JMJD2) family of proteins, and demonstrate its binding to both class I...

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Autores:
Gray, Steven G.
Iglesias, Antonio H.
Lizcano Losada, Fernando
Villanueva, Raul
Camelo, Sandra
Jingu, Hisaka
Teh T., Bin
Koibuchi, Noriyuki
W. Chin, William
Kokkotou, Efi
Dangond, Fernando
Tipo de recurso:
Fecha de publicación:
2005
Institución:
Universidad de la Sabana
Repositorio:
Repositorio Universidad de la Sabana
Idioma:
eng
OAI Identifier:
oai:intellectum.unisabana.edu.co:10818/22629
Acceso en línea:
http://www.jbc.org/content/280/31/28507.full.pdf+html
http://hdl.handle.net/10818/22629
Palabra clave:
Retinoblastoma
Neoplasmas de los ojos
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License
Attribution-NonCommercial-NoDerivatives 4.0 International
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spelling Gray, Steven G.Iglesias, Antonio H.Lizcano Losada, FernandoVillanueva, RaulCamelo, SandraJingu, HisakaTeh T., BinKoibuchi, NoriyukiW. Chin, WilliamKokkotou, EfiDangond, Fernando3/15/2016 16:542016-03-15T21:54:23Z2005-05-3128507–28518http://www.jbc.org/content/280/31/28507.full.pdf+htmlhttp://hdl.handle.net/10818/22629To effectively direct targeted repression, the class I histone deacetylases (HDACs) associate with many important regulatory proteins. In this paper we describe the molecular characterization of a member of the Jumonji domain 2 (JMJD2) family of proteins, and demonstrate its binding to both class I HDACs and the retinoblastoma protein (pRb). JMJD2 proteins are characterized by the presence of two leukemia-associated protein/plant homeodomain (LAP/PHD) zinc fingers, one JmjN, one JmjC (containing an internal retinoblastoma-binding protein 2 (RBBP2)-like sequence), and two Tudor domains. The first member of this group, JMJD2A, is widely expressed in human tissues and cell lines, and high endogenous expression of JMJD2A mRNA was found in several cell types, including human T-cell lymphotropic virus 1 (HTLV-1)-infected cell lines. JMJD2A and JMJD2B exhibit cell type-specific responses to the HDAC inhibitor trichostatin A. We show that the JMJD2A protein associates in vivo with pRb and class I HDACs, and mediates repression of E2F-regulated promoters. In HTLV-1 virus-infected cells, we find that JMJD2A binds to the viral Tax protein. Antibodies to JMJD2A recognize the native protein but also a half-sized protein fragment, the latter up-regulated in THP-1 cells during the G2/M phase of the cell cycle. The ability of JMJD2A to associate with pRb and HDACs and potentiate pRb-mediated repression of E2F-regulated promoters implies an important role for this protein in cell proliferation and oncogenesis.Según Sherpa Romeo el autor no puede archivar la versión del editor / PDFapplication/pdfengThe Journal of Biological ChemistryThe Journal of Biological Chemistry Vol. 280, No. 31 p. 28507–28518 de 2005Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/http://purl.org/coar/access_right/c_abf2Universidad de La SabanaIntellectum Repositorio Universidad de La SabanaRetinoblastomaNeoplasmas de los ojosFunctional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding proteinarticlepublishedVersionhttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-81223https://intellectum.unisabana.edu.co/bitstream/10818/22629/2/license_rdf7c9ab7f006165862d8ce9ac5eac01552MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-8498https://intellectum.unisabana.edu.co/bitstream/10818/22629/3/license.txtf52a2cfd4df262e08e9b300d62c85cabMD5310818/22629oai:intellectum.unisabana.edu.co:10818/226292022-05-10 05:16:03.565Intellectum Universidad de la Sabanacontactointellectum@unisabana.edu.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
dc.title.es_CO.fl_str_mv Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
title Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
spellingShingle Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
Retinoblastoma
Neoplasmas de los ojos
title_short Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
title_full Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
title_fullStr Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
title_full_unstemmed Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
title_sort Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
dc.creator.fl_str_mv Gray, Steven G.
Iglesias, Antonio H.
Lizcano Losada, Fernando
Villanueva, Raul
Camelo, Sandra
Jingu, Hisaka
Teh T., Bin
Koibuchi, Noriyuki
W. Chin, William
Kokkotou, Efi
Dangond, Fernando
dc.contributor.author.none.fl_str_mv Gray, Steven G.
Iglesias, Antonio H.
Lizcano Losada, Fernando
Villanueva, Raul
Camelo, Sandra
Jingu, Hisaka
Teh T., Bin
Koibuchi, Noriyuki
W. Chin, William
Kokkotou, Efi
Dangond, Fernando
dc.subject.other.es_CO.fl_str_mv Retinoblastoma
Neoplasmas de los ojos
topic Retinoblastoma
Neoplasmas de los ojos
description To effectively direct targeted repression, the class I histone deacetylases (HDACs) associate with many important regulatory proteins. In this paper we describe the molecular characterization of a member of the Jumonji domain 2 (JMJD2) family of proteins, and demonstrate its binding to both class I HDACs and the retinoblastoma protein (pRb). JMJD2 proteins are characterized by the presence of two leukemia-associated protein/plant homeodomain (LAP/PHD) zinc fingers, one JmjN, one JmjC (containing an internal retinoblastoma-binding protein 2 (RBBP2)-like sequence), and two Tudor domains. The first member of this group, JMJD2A, is widely expressed in human tissues and cell lines, and high endogenous expression of JMJD2A mRNA was found in several cell types, including human T-cell lymphotropic virus 1 (HTLV-1)-infected cell lines. JMJD2A and JMJD2B exhibit cell type-specific responses to the HDAC inhibitor trichostatin A. We show that the JMJD2A protein associates in vivo with pRb and class I HDACs, and mediates repression of E2F-regulated promoters. In HTLV-1 virus-infected cells, we find that JMJD2A binds to the viral Tax protein. Antibodies to JMJD2A recognize the native protein but also a half-sized protein fragment, the latter up-regulated in THP-1 cells during the G2/M phase of the cell cycle. The ability of JMJD2A to associate with pRb and HDACs and potentiate pRb-mediated repression of E2F-regulated promoters implies an important role for this protein in cell proliferation and oncogenesis.
publishDate 2005
dc.date.issued.none.fl_str_mv 2005-05-31
dc.date.available.none.fl_str_mv 2016-03-15T21:54:23Z
dc.date.accessioned.none.fl_str_mv 3/15/2016 16:54
dc.type.en.fl_str_mv article
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dc.identifier.issn.none.fl_str_mv 28507–28518
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dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/10818/22629
identifier_str_mv 28507–28518
url http://www.jbc.org/content/280/31/28507.full.pdf+html
http://hdl.handle.net/10818/22629
dc.language.iso.es_CO.fl_str_mv eng
language eng
dc.relation.ispartofseries.none.fl_str_mv The Journal of Biological Chemistry Vol. 280, No. 31 p. 28507–28518 de 2005
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http://creativecommons.org/licenses/by-nc-nd/4.0/
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dc.publisher.es_CO.fl_str_mv The Journal of Biological Chemistry
dc.source.es_CO.fl_str_mv Universidad de La Sabana
Intellectum Repositorio Universidad de La Sabana
institution Universidad de la Sabana
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