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...
- 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
- Rights
- License
- Attribution-NonCommercial-NoDerivatives 4.0 International
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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.coPGEgcmVsPSJsaWNlbnNlIiBocmVmPSJodHRwOi8vY3JlYXRpdmVjb21tb25zLm9yZy9saWNlbnNlcy9ieS1uYy1uZC8zLjAvIj48aW1nIGFsdD0iTGljZW5jaWEgQ3JlYXRpdmUgQ29tbW9ucyIgc3R5bGU9ImJvcmRlci13aWR0aDowIiBzcmM9Imh0dHA6Ly9pLmNyZWF0aXZlY29tbW9ucy5vcmcvbC9ieS1uYy1uZC8zLjAvODh4MzEucG5nIiAvPjwvYT48YnIgLz5Fc3RlIDxzcGFuIHhtbG5zOmRjdD0iaHR0cDovL3B1cmwub3JnL2RjL3Rlcm1zLyIgaHJlZj0iaHR0cDovL3B1cmwub3JnL2RjL2RjbWl0eXBlL1RleHQiIHJlbD0iZGN0OnR5cGUiPm9icmE8L3NwYW4+IGVzdMOhIGJham8gdW5hIDxhIHJlbD0ibGljZW5zZSIgaHJlZj0iaHR0cDovL2NyZWF0aXZlY29tbW9ucy5vcmcvbGljZW5zZXMvYnktbmMtbmQvMy4wLyI+bGljZW5jaWEgQ3JlYXRpdmUgQ29tbW9ucyBSZWNvbm9jaW1pZW50by1Ob0NvbWVyY2lhbC1TaW5PYnJhRGVyaXZhZGEgMy4wIFVucG9ydGVkPC9hPi4K |
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 |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.coar.fl_str_mv |
http://purl.org/coar/resource_type/c_6501 |
dc.type.hasVersion.es_CO.fl_str_mv |
publishedVersion |
dc.identifier.issn.none.fl_str_mv |
28507–28518 |
dc.identifier.other.none.fl_str_mv |
http://www.jbc.org/content/280/31/28507.full.pdf+html |
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 |
dc.rights.*.fl_str_mv |
Attribution-NonCommercial-NoDerivatives 4.0 International |
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http://purl.org/coar/access_right/c_abf2 |
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http://creativecommons.org/licenses/by-nc-nd/4.0/ |
rights_invalid_str_mv |
Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/ http://purl.org/coar/access_right/c_abf2 |
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application/pdf |
dc.publisher.es_CO.fl_str_mv |
The Journal of Biological Chemistry |
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Universidad de La Sabana Intellectum Repositorio Universidad de La Sabana |
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Universidad de la Sabana |
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