Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Targeting Lysine Demethylase 5 (KDM5) in Mantle Cell Lymphoma

ABSTRACT: Targeting Lysine Demethylase 5 (KDM5) in Mantle Cell Lymphoma

PROVIDER: PRJNA1018417 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

Targeting Lysine Demethylase 5 (KDM5) in Mantle Cell Lymphoma

Project description:Loss of function mutations in the histone methyltransferase KMT2D are common in lymphomas but difficult to target. We reported targeting KDM5 restores epigenetic balance in germinal centre (GC) lymphomas. Here, we show the KDM5 family are over-expressed in mantle cell lymphoma (MCL). GS716054, a pro-drug, increases H3K4 trimethylation (H3K4me3) and kills MCL cells including TP53 mutated cells via suppression of the MYC pathway. It can overcome ibrutinib resistance and synergises with ibrutinib. These data suggest a possible role for KDM5-inhibitors in advanced MCL.

2024-09-24 | GSE243395 | GEO

Targeting lysine demethylase 5 (KDM5) in mantle cell lymphoma.

Project description: Not available

| S-EPMC10864367 | biostudies-literature

KDM5 Lysine Demethylases Are Involved in Maintenance of 3'UTR Length [ChIP-Seq]

Project description:We discovered that the Saccharomyces cerevisiae lysine demethylase, Jhd2 (also known as KDM5), recruits 3'UTR processing machinery and promotes alteration of 3'UTR length in a demethylase-dependent manner. Interaction of Jhd2 with both chromatin and RNA suggests that Jhd2 affects selection of polyadenylation sites through a transcription-coupled mechanism. Wild-type yeast or yeast with JHD2 deleted were grown to mid-log phase. ChIP analysis performed for H3K4me3, Pol2, IgG.

2016-03-23 | E-GEOD-67211 | biostudies-arrayexpress

Non-canonical RNA-binding of the histone lysine demethylase KDM5 through interactions with G-quadruplex sequences

Project description:RNA-binding proteins are important regulators of RNA biogenesis and function, and recent work shows that chromatin- and RNA-binding proteins can have regulatory roles in transcription. Several approaches have been developed to predict RNA-binding proteins and to identify them experimentally at large scale, including binding to structural elements as G-quadruplexes. Here, we show that the histone lysine demethylase protein KDM5 can bind to RNA through interaction with G-quadruplexes with high affinity despite neither being categorized as an RNA-binding protein nor identified as a G-quadruplex binding protein across numerous experimental large-scale and computational studies. In addition to characterizing the KDM5 G-quadruplex interaction we show that RNA is directly involved in the formation of KDM5-containing protein complexes. Computational predictions and comparison to other ARID domain containing proteins suggest that the ARID domain is directly interacting with both DNA and RNA across several proteins. Our work highlights that non-canonical aspects of RNA-binding proteins are present, and that G-quadruplex RNA-binding could provide a regulatory mechanism for chromatin-binding proteins with impact on transcription through linking protein complexes within the cell.

2024-04-11 | PXD050767 | Pride

KDM5 Lysine Demethylases Are Involved in Maintenance of 3'UTR Length [ChIP-Seq]

2016-03-23 | GSE67211 | GEO

KDM5 Lysine Demethylases Are Involved in Maintenance of 3'UTR Length [RNA-Seq]

2016-03-23 | GSE67163 | GEO

Proteaphagy contributes to bortezomib resistance in mantle cell lymphoma

Project description:TUBE and GST enrichment followed by 1D-gel-LC-MS analysis on cell exract from bortezomib (BTZ)-resistant or sensitive mantle cell lymphoma cells.

2022-02-28 | PXD011867 | Pride

ibrutinib resistance mantle cell lymphoma

Project description:ibrutinib resistance mantle cell lymphoma

| PRJNA593190 | ENA

Targeted DamID analyses of neural progenitor cells and immature neurons of kdm5[140] and kdm5 shRNA Drosophila larvae and pupae.

Project description:Mutations in the lysine demethylase 5 (KDM5) family of transcriptional regulators are associated with intellectual disability, yet little is known regarding their spatiotemporal requirements or neurodevelopmental contributions. Utilizing the mushroom body (MB), a major learning and memory center within the Drosophila brain, we demonstrate that KDM5 is required within ganglion mother cells and immature neurons for proper axogenesis. Moreover, the mechanism by which KDM5 functions in this context is independent of its canonical histone demethylase activity. Using in vivo transcriptional and binding analyses, we identify a network of genes directly regulated by KDM5 that are critical modulators of neurodevelopment. We find that KDM5 directly regulates the expression of prospero, a transcription factor that we demonstrate is essential for MB morphogenesis. Prospero functions downstream of KDM5 and binds to approximately half of KDM5-regulated genes. Together, our data provide evidence for a KDM5-Prospero transcriptional axis that is essential for proper MB development.

2021-03-16 | GSE156010 | GEO

KDM5 histone demethylases repress innate immune response via suppression of STING

Project description:Tri-methylation on histone H3 lysine 4 (H3K4me3) is enriched near transcription start sites and correlates with active transcription. Like other histone marks, methylation on H3K4 is catalyzed by the respective methyltransferases and erased by demethylases. Lysine demethylase 5 (KDM5) family of Fe (II) and α-ketoglutarate-dependent dioxygenases removes the methyl groups from H3K4me3. All four family members of KDM5 demethylases (KDM5A-D) share sequence identity, have similar in vitro kinetic parameters, and display functional redundancy. To determine the effects of complete depletion of KDM5 activity, we treated MCF7 cells with DMSO, or two pan-KDM5 specific inhibitors, KDM5-C70 (our lab code 443) and CPI-48 (our lab code 278) and performed RNA sequencing to determine gene expression changes after KDM5 inhibitor treatment.

2018-07-03 | GSE108502 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data