JmjC-domain-containing proteins and histone demethylation

Klose, Robert J.; Kallin, Eric M.; Zhang, Yi

doi:10.1038/nrg1945

Cited by 1,125 publications

(1,174 citation statements)

References 97 publications

Supporting

Mentioning

1,143

Contrasting

Unclassified

Order By: Relevance

“…It will be of great interest to experimentally address to which extent the post-translational modifications of the NF-kB/IkB proteins themselves in response to various signals ultimately regulate the ability of those transcription factors to recruit H3K4 HMT complexes on the promoters of their target genes. H3K4 me3 is a dynamic modification (Berger, 2007) and a family of proteins sharing the Jumonji C (JmjC) domain were showed to catalyse site-specific demethylation of mono-, di-and trimethylated histones (Klose et al, 2006). Among them is RBP2, a demethylase that specifically catalyses demethylation on H3K4 (Klose et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

et al. 2009

View full text Add to dashboard Cite

Constitutive nuclear factor (NF)-jB activation in haematological malignancies is caused in several cases by loss of function mutations within the coding sequence of NF-jB inhibitory molecules such as IjBa or p100. Hut-78, a truncated form of p100, constitutively generates p52 and contributes to the development of T-cell lymphomas but the molecular mechanism underlying this oncogenic potential remains unclear. We show here that MMP9 gene expression is induced through the alternative NF-jB-activating pathway in fibroblasts and also on Hut-78 or p52 overexpression in fibroblasts as well as in lymphoma cells. p52 is critical for Hut-78-mediated MMP9 gene induction as a Hut-78 mutant as well as other truncated NF-jB2 proteins that are not processed into p52 failed to induce the expression of this metalloproteinase. Conversely, MMP9 gene expression is impaired in p52-depleted HUT-78 cells. Interestingly, MLL1 and MLL2 H3K4 methyltransferase complexes are tethered by p52 on the MMP9 but not on the IjBa promoter, and the H3K4 trimethyltransferase activity recruited on the MMP9 promoter is impaired in p52-depleted HUT-78 cells. Moreover, MLL1 and MLL2 are associated with Hut-78 in a native chromatin-enriched extract. Thus, we identified a molecular mechanism by which the recruitment of a H3K4 histone methyltransferase complex on the promoter of a NF-jB-dependent gene induces its expression and potentially the invasive potential of lymphoma cells harbouring constitutive activity of the alternative NF-jB-activating pathway.

show abstract

Section: Discussionmentioning

confidence: 99%

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

et al. 2009

View full text Add to dashboard Cite

show abstract

“…Methylation has been shown to occur on five K residues of histone H3 (K4, K9, K27, K36 and K79), and on four R residues (R2, R8, R17 and R26). H4K20 and H4R3 are also methylated [1,2]. Methylation is a reversible modification regulated by site-specific methyltransferases and demethylases [1].…”

mentioning

confidence: 99%

Features of the PHF8/KIAA1718 histone demethylase

Suganuma

Workman

2010

Cell Res

View full text Add to dashboard Cite

“…As of today, three classes of histone demethylases have been identified (Klose et al 2006). The largest class of demethylase enzymes contains a Jumonji C (JmjC) domain.…”

Section: Methylation Of Histonesmentioning

confidence: 99%

Nutrition, Histone Epigenetic Marks, and Disease

Zempleni

Liu

Xue

2013

Environmental Epigenomics in Health and Disease

View full text Add to dashboard Cite

The dietary intake of essential nutrients and bioactive food compounds is a process that occurs on a daily basis for the entire life span. Therefore, your diet has a great potential to cause changes in the epigenome. Known histone modifications include acetylation, methylation, biotinylation, poly(ADP-ribosylation), ubiquitination, and sumoylation. Some of these modifications depend directly on dietary nutrients. For other modifications, bioactive dietary compounds may alter the activities of enzymes that establish or remove histone marks, thereby altering the epigenome. This chapter provides an overview of diet-dependent epigenomic marks in histones and their links with human health.

show abstract

JmjC-domain-containing proteins and histone demethylation

Cited by 1,125 publications

References 97 publications

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

Matrix Metalloproteinase-9 gene induction by a truncated oncogenic NF-κB2 protein involves the recruitment of MLL1 and MLL2 H3K4 histone methyltransferase complexes

Features of the PHF8/KIAA1718 histone demethylase

Nutrition, Histone Epigenetic Marks, and Disease

Contact Info

Product

Resources

About