The enzymes catalyzing lysine and arginine methylation of histones
are essential for maintaining transcriptional programs and determining
cell fate and identity. Until recently, histone methylation was regarded
irreversible. However, within the last few years, several families
of histone demethylases erasing methyl marks associated with gene
repression or activation have been identified, underscoring the plasticity
and dynamic nature of histone methylation. Recent discoveries have
revealed that histone demethylases take part in large multiprotein
complexes synergizing with histone deacetylases, histone methyltransferases,
and nuclear receptors to control developmental and transcriptional
programs. Here we review the emerging biochemical and biological
functions of the histone demethylases and discuss their potential
involvement in human diseases, including cancer.
%0 Journal Article
%1 Cloos08
%A Cloos, Paul A C
%A Christensen, Jesper
%A Agger, Karl
%A Helin, Kristian
%D 2008
%J Genes Dev.
%K Aging Animals Cell_Differentiation Histones,_metabolism Humans Methylation Models,_Biological Neoplasms,_metabolism/pathology Oxidoreductases,_N-Demethylating,_classification/metabolism Phylogeny
%N 9
%P 1115-40
%R 10.1101/gad.1652908
%T Erasing the methyl mark: histone demethylases at the center of cellular
differentiation and disease.
%U http://dx.doi.org/10.1101/gad.1652908
%V 22
%X The enzymes catalyzing lysine and arginine methylation of histones
are essential for maintaining transcriptional programs and determining
cell fate and identity. Until recently, histone methylation was regarded
irreversible. However, within the last few years, several families
of histone demethylases erasing methyl marks associated with gene
repression or activation have been identified, underscoring the plasticity
and dynamic nature of histone methylation. Recent discoveries have
revealed that histone demethylases take part in large multiprotein
complexes synergizing with histone deacetylases, histone methyltransferases,
and nuclear receptors to control developmental and transcriptional
programs. Here we review the emerging biochemical and biological
functions of the histone demethylases and discuss their potential
involvement in human diseases, including cancer.
@article{Cloos08,
abstract = {The enzymes catalyzing lysine and arginine methylation of histones
are essential for maintaining transcriptional programs and determining
cell fate and identity. Until recently, histone methylation was regarded
irreversible. However, within the last few years, several families
of histone demethylases erasing methyl marks associated with gene
repression or activation have been identified, underscoring the plasticity
and dynamic nature of histone methylation. Recent discoveries have
revealed that histone demethylases take part in large multiprotein
complexes synergizing with histone deacetylases, histone methyltransferases,
and nuclear receptors to control developmental and transcriptional
programs. Here we review the emerging biochemical and biological
functions of the histone demethylases and discuss their potential
involvement in human diseases, including cancer.},
added-at = {2010-01-26T20:35:53.000+0100},
author = {Cloos, Paul A C and Christensen, Jesper and Agger, Karl and Helin, Kristian},
biburl = {https://www.bibsonomy.org/bibtex/2d660b9d5c0cd6a979758baa05a15b8e5/denilw},
doi = {10.1101/gad.1652908},
file = {article:../Histone modifications/Erasing the methyl mark%3A histone
demethylases at the center of cellular differentiation and disease.pdf:pdf},
institution = {Biotech Research and Innovation Centre, University of Copenhagen,
DK-2200 Copenhagen, Denmark. paul.cloos@bric.dk},
interhash = {22a25543c74be29ad575ac6e17787c2c},
intrahash = {d660b9d5c0cd6a979758baa05a15b8e5},
journal = {Genes Dev.},
keywords = {Aging Animals Cell_Differentiation Histones,_metabolism Humans Methylation Models,_Biological Neoplasms,_metabolism/pathology Oxidoreductases,_N-Demethylating,_classification/metabolism Phylogeny},
month = May,
number = 9,
owner = {denilw},
pages = {1115-40},
pii = {22/9/1115},
pmid = {18451103},
timestamp = {2010-01-26T20:35:56.000+0100},
title = {Erasing the methyl mark: histone demethylases at the center of cellular
differentiation and disease.},
url = {http://dx.doi.org/10.1101/gad.1652908},
volume = 22,
year = 2008
}