g6919

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Showing 1-19 of 19 results for "g6919" within Papers

Methylation of hypoxia-inducible factor (HIF)-1 alpha by G9a/GLP inhibits HIF-1 transcriptional activity and cell migration

Bao L, et al.

Nucleic Acids Research, 46(13), 6576-6591 (2018)

Inhibition of the H3K9 methyltransferase G9A attenuates oncogenicity and activates the hypoxia signaling pathway.

Jolene Caifeng Ho et al.

PloS one, 12(11), e0188051-e0188051 (2017-11-18)

Epigenetic mechanisms play important roles in the regulation of tumorigenesis, and hypoxia-induced epigenetic changes may be critical for the adaptation of cancer cells to the hypoxic microenvironment of solid tumors. Previously, we showed that loss-of-function of the hypoxia-regulated H3K9 methyltransferase

Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains.

Judd C Rice et al.

Molecular cell, 12(6), 1591-1598 (2003-12-24)

The functional significance of mono-, di-, and trimethylation of lysine residues within histone proteins remains unclear. Antibodies developed to selectively recognize each of these methylated states at histone H3 lysine 9 (H3 Lys9) demonstrated that mono- and dimethylation localized specifically

G9a-mediated methylation of ERα links the PHF20/MOF histone acetyltransferase complex to hormonal gene expression.

Xi Zhang et al.

Nature communications, 7, 10810-10810 (2016-03-11)

The euchromatin histone methyltransferase 2 (also known as G9a) methylates histone H3K9 to repress gene expression, but it also acts as a coactivator for some nuclear receptors. The molecular mechanisms underlying this activation remain elusive. Here we show that G9a

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis.

Makoto Tachibana et al.

Genes & development, 16(14), 1779-1791 (2002-07-20)

Covalent modification of histone tails is crucial for transcriptional regulation, mitotic chromosomal condensation, and heterochromatin formation. Histone H3 lysine 9 (H3-K9) methylation catalyzed by the Suv39h family proteins is essential for establishing the architecture of pericentric heterochromatin. We recently identified

Increasing G9a automethylation sensitizes B acute lymphoblastic leukemia cells to glucocorticoid-induced death.

Coralie Poulard et al.

Cell death & disease, 9(10), 1038-1038 (2018-10-12)

Synthetic glucocorticoids (GCs) are used to treat lymphoid cancers, but many patients develop resistance to treatment, especially to GC. By identifying genes that influence sensitivity to GC-induced cell death, we found that histone methyltransferases G9a and G9a-like protein (GLP), two

GLP-catalyzed H4K16me1 promotes 53BP1 recruitment to permit DNA damage repair and cell survival.

Xiaopeng Lu et al.

Nucleic acids research, 47(21), 10977-10993 (2019-10-16)

The binding of p53-binding protein 1 (53BP1) to damaged chromatin is a critical event in non-homologous DNA end joining (NHEJ)-mediated DNA damage repair. Although several molecular pathways explaining how 53BP1 binds damaged chromatin have been described, the precise underlying mechanisms

EHMT2 inhibitor BIX-01294 induces apoptosis through PMAIP1-USP9X-MCL1 axis in human bladder cancer cells.

Jing Cui et al.

Cancer cell international, 15(1), 4-4 (2015-02-17)

BIX-01294, an euchromatic histone-lysine N-methyltransferase 2 (EHMT2) inhibitor, has been reported to induce apoptosis in human neuroblastoma cells and inhibit the proliferation of bladder cancer cells. However, the definite mechanism of the apoptosis mediated by BIX-01294 in bladder cancer cells

Lysine methyltransferase G9a is not required for DNMT3A/3B anchoring to methylated nucleosomes and maintenance of DNA methylation in somatic cells.

Shikhar Sharma et al.

Epigenetics & chromatin, 5(1), 3-3 (2012-01-31)

DNA methylation, histone modifications and nucleosome occupancy act in concert for regulation of gene expression patterns in mammalian cells. Recently, G9a, a H3K9 methyltransferase, has been shown to play a role in establishment of DNA methylation at embryonic gene targets

A post-translational modification switch controls coactivator function of histone methyltransferases G9a and GLP.

Coralie Poulard et al.

EMBO reports, 18(8), 1442-1459 (2017-06-16)

Like many transcription regulators, histone methyltransferases G9a and G9a-like protein (GLP) can act gene-specifically as coregulators, but mechanisms controlling this specificity are mostly unknown. We show that adjacent post-translational methylation and phosphorylation regulate binding of G9a and GLP to heterochromatin

Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3.

M Tachibana et al.

The Journal of biological chemistry, 276(27), 25309-25317 (2001-04-24)

The covalent modification of histone tails has regulatory roles in various nuclear processes, such as control of transcription and mitotic chromosome condensation. Among the different groups of enzymes known to catalyze the covalent modification, the most recent additions are the

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis

Tachibana M, et al.

Genes, 16(14), 1779-1779 (2002)

Epigenetic response to environmental stress: Assembly of BRG1-G9a/GLP-DNMT3 repressive chromatin complex on Myh6 promoter in pathologically stressed hearts.

Pei Han et al.

Biochimica et biophysica acta, 1863(7 Pt B), 1772-1781 (2016-03-10)

Chromatin structure is determined by nucleosome positioning, histone modifications, and DNA methylation. How chromatin modifications are coordinately altered under pathological conditions remains elusive. Here we describe a stress-activated mechanism of concerted chromatin modification in the heart. In mice, pathological stress

Inhibition of the H3K9 methyltransferase G9A attenuates oncogenicity and activates the hypoxia signaling pathway

Ho JC, et al.

PLoS ONE, 12(11), e0188051-e0188051 (2017)

The Lysine Methyltransferase G9a in Immune Cell Differentiation and Function

Scheer S, et al.

Frontiers in Immunology, 8 (2017)

Coordinated histone modifications mediated by a CtBP co-repressor complex.

Yujiang Shi et al.

Nature, 422(6933), 735-738 (2003-04-18)

The transcriptional co-repressor CtBP (C-terminal binding protein) is implicated in tumorigenesis because it is targeted by the adenovirus E1A protein during oncogenic transformation. Genetic studies have also identified a crucial function for CtBP in animal development. CtBP is recruited to

A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.

Hidesato Ogawa et al.

Science (New York, N.Y.), 296(5570), 1132-1136 (2002-05-11)

E2F-6 contributes to gene silencing in a manner independent of retinoblastoma protein family members. To better elucidate the molecular mechanism of repression by E2F-6, we have purified the factor from cultured cells. E2F-6 is found in a multimeric protein complex

Methylation of hypoxia-inducible factor (HIF)-1α by G9a/GLP inhibits HIF-1 transcriptional activity and cell migration.

Lei Bao et al.

Nucleic acids research, 46(13), 6576-6591 (2018-06-04)

Hypoxia-inducible factor 1 (HIF-1) is a master transcriptional regulator in response to hypoxia and its transcriptional activity is crucial for cancer cell mobility. Here we present evidence for a novel epigenetic mechanism that regulates HIF-1 transcriptional activity and HIF-1-dependent migration

Study of methyl transferase (G9aMT) and methylated histone (H3-K9) expressions in unexplained recurrent spontaneous abortion (URSA) and normal early pregnancy

Fatima N, et al.

Molecular Human Reproduction, 17(11), 693-701 (2011)

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