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Physiological Roles of Class I HDAC Complex and Histone Demethylase

Epigenetic gene silencing is one of the fundamental mechanisms for ensuring proper gene expression patterns during cellular differentiation and development. Histone deacetylases (HDACs) are evolutionally conserved enzymes that remove acetyl modifications from histones and play a central role in epig...

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Detalles Bibliográficos
Autores principales: Hayakawa, Tomohiro, Nakayama, Jun-ichi
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2964911/
https://www.ncbi.nlm.nih.gov/pubmed/21049000
http://dx.doi.org/10.1155/2011/129383
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author Hayakawa, Tomohiro
Nakayama, Jun-ichi
author_facet Hayakawa, Tomohiro
Nakayama, Jun-ichi
author_sort Hayakawa, Tomohiro
collection PubMed
description Epigenetic gene silencing is one of the fundamental mechanisms for ensuring proper gene expression patterns during cellular differentiation and development. Histone deacetylases (HDACs) are evolutionally conserved enzymes that remove acetyl modifications from histones and play a central role in epigenetic gene silencing. In cells, HDAC forms a multiprotein complex (HDAC complex) in which the associated proteins are believed to help HDAC carry out its cellular functions. Though each HDAC complex contains distinct components, the presence of isoforms for some of the components expands the variety of complexes and the diversity of their cellular roles. Recent studies have also revealed a functional link between HDAC complexes and specific histone demethylases. In this paper, we summarize the distinct and cooperative roles of four class I HDAC complexes, Sin3, NuRD, CoREST, and NCoR/SMRT, with respect to their component diversity and their relationship with specific histone demethylases.
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spelling pubmed-29649112010-11-03 Physiological Roles of Class I HDAC Complex and Histone Demethylase Hayakawa, Tomohiro Nakayama, Jun-ichi J Biomed Biotechnol Review Article Epigenetic gene silencing is one of the fundamental mechanisms for ensuring proper gene expression patterns during cellular differentiation and development. Histone deacetylases (HDACs) are evolutionally conserved enzymes that remove acetyl modifications from histones and play a central role in epigenetic gene silencing. In cells, HDAC forms a multiprotein complex (HDAC complex) in which the associated proteins are believed to help HDAC carry out its cellular functions. Though each HDAC complex contains distinct components, the presence of isoforms for some of the components expands the variety of complexes and the diversity of their cellular roles. Recent studies have also revealed a functional link between HDAC complexes and specific histone demethylases. In this paper, we summarize the distinct and cooperative roles of four class I HDAC complexes, Sin3, NuRD, CoREST, and NCoR/SMRT, with respect to their component diversity and their relationship with specific histone demethylases. Hindawi Publishing Corporation 2011 2010-10-26 /pmc/articles/PMC2964911/ /pubmed/21049000 http://dx.doi.org/10.1155/2011/129383 Text en Copyright © 2011 T. Hayakawa and J.-i. Nakayama. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Hayakawa, Tomohiro
Nakayama, Jun-ichi
Physiological Roles of Class I HDAC Complex and Histone Demethylase
title Physiological Roles of Class I HDAC Complex and Histone Demethylase
title_full Physiological Roles of Class I HDAC Complex and Histone Demethylase
title_fullStr Physiological Roles of Class I HDAC Complex and Histone Demethylase
title_full_unstemmed Physiological Roles of Class I HDAC Complex and Histone Demethylase
title_short Physiological Roles of Class I HDAC Complex and Histone Demethylase
title_sort physiological roles of class i hdac complex and histone demethylase
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2964911/
https://www.ncbi.nlm.nih.gov/pubmed/21049000
http://dx.doi.org/10.1155/2011/129383
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