Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

FBP1 acts as a protein phosphatase to dephosphorylate histone H3

ABSTRACT: FBP1 acts as a protein phosphatase to dephosphorylate histone H3

PROVIDER: PRJNA857428 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR20073501_1.fastq.gz	Fastqsanger.gz
	SRR20073501_2.fastq.gz	Fastqsanger.gz
	SRR20073502_1.fastq.gz	Fastqsanger.gz
	SRR20073502_2.fastq.gz	Fastqsanger.gz

Items per page:

1 - 4 of 4

Similar Datasets

FBP1 acts as a protein phosphatase to dephosphorylate histone H3

Project description:We report nuclear FBP1 interacts with PPARa and binds to the promoter regions of PPARa-mediated b-oxidation genes. S170-phosphorylated FBP1 with an altered catalytic domain structure functions as a protein phosphatase that dephosphorylates histone H3 at T11 and suppresses PPARa-mediated gene expression. Chromatin immunoprecipitation DNA-sequencing (ChIP-seq) for FBP1 and PPARa with glucose deprivation in L02 cells.

2022-10-04 | GSE207844 | GEO

UBR7 Acts as a Chaperone for Post-Nucleosomal Histone H3

Project description:UBR7 Acts as a Chaperone for Post-Nucleosomal Histone H3

| PRJNA761773 | ENA

FBP1 associated proteins: FBP1 immunoprecipitants

Project description:To determine whether FBP1 has previously unknown tumor suppressor activity, we immunoprecipitated FBP1 from Huh7 HCC cells and performed mass spectrometry analyses of FBP1 immunoprecipitants.

2024-03-12 | PXD050213 | Pride

FBP1 overexpression in MDA-MB-231 breast cancer cells

Project description:Fructose 1,6 bisphosphatase the key enzyme of gluconeogenesis has emerged as a potential metabolic tumor suppressor. In breast cancer distinct FBP1 expression levels are found depending on subtype. In MDA-MB-231 FBP1 expression is suppressed. To get more insight into potential functions of FBP1 we introduced a vector to reintroduce expression of FBP1. These experiments are part of a more comprehensive study on expression of FBP1 in breast cancer cells.

2023-10-02 | GSE244288 | GEO

An EZH2-FBP1 Feedback Circuitry Promotes Tumorigenesis in Gluconeogenic Tissues

Project description:We report that enhancer of zeste homologue 2 (EZH2) represses the expression of a rate-limiting gluconeogenic enzyme fructose-1, 6 -bisphosphatase 1 (FBP1) to promote tumorigenesis. More intriguingly, FBP1 inhibits EZH2 methyltransferase activity by binding EZH2 at targeted loci and dissembles the polycomb complex, which constitutes a negative feedback loop for EZH2-initiated signalings. We performed ChIP-Seq assays using the EZH2 and H3K27me3 antibody in HCC cells with vector control, FBP1 wild-type (WT) or FBP1 S169A re-expression. FBP1 WT severely reduced EZH2 and H3K27me3 signals. Conversely, FBP1 S169A exhibits much less effects on global or target-specific H3K27me3. In addition, ChIP-Seq assays with the FBP1 uncover a significant overlap between EZH2 and FBP1 binding sites, confirming that FBP1 inhibits EZH2 though physical interactions in the vicinity of chromosomes. Collectively, these studies reveal an unexpected crosstalk between metabolic and epigenetic events, and identify a new mechanistic circuitry highlighting EZH2 inhibitors as liver and kidney cancer therapeutics.

2019-03-12 | GSE128137 | GEO

Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation

Project description:Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation. Middle down analysis of histone H3 WT or mutant

2023-07-27 | MSV000092535 | MassIVE

Identification of ubiquitination sites of purified histone H3

Project description:Histones modulate gene expression by chromatin compaction, regulating numerous processes such as differentiation. However, the mechanisms underlying histone degradation remain elusive. When compared with their differentiated counterparts, immortal human embryonic stem cells (hESCs) have a unique chromatin architecture and low levels of trimethylated histone H3 at lysine 9 (H3K9me3), a heterochromatin-associated modification. Here we assess a link between the intrinsic epigenetic landscape and ubiquitin-proteasome system of hESCs. We find that hESCs exhibit high expression of UBE2K, a ubiquitin-conjugating enzyme. Loss of UBE2K increases the levels of H3K9 trimethyltransferase SETDB1, resulting in H3K9 trimethylation and repression of neurogenic genes during differentiation. Concomitantly, loss of UBE2K impairs the ability of hESCs to differentiate into neural progenitors with neurogenic properties. Besides H3K9 trimethylation, we find that UBE2K binds histone H3 to induce its polyubiquitination and degradation by the proteasome. Notably, ubc-20, the worm orthologue of UBE2K, also regulates both histone H3 levels and H3K9 trimethylation in C. elegans germline. Thus, our results indicate that UBE2K crosses evolutionary boundaries to promote histone H3 degradation and reduce H3K9me3 repressive marks in immortal cells.

2020-06-01 | PXD018621 | Pride

FBP1 expression in basal-like breast cancer MDA-MB231 and Hs578T cells

Project description:FBP1 is a rate limiting enzyme in glucogenogenesis and FBP1 expression changes cells to oxidative phosphorylation. Expressing FBP1 in basal-like breast cancer cells, which lack the expression of this enzyme, will identify the genes involved in glycolysis. FBP1 was expressed in MDA-MB231 and Hs578T cells, stable clones were selected, and RNA was prepared for microarray analysis.

2012-09-27 | E-GEOD-41158 | biostudies-arrayexpress

UBR7 Acts as a Chaperone for Post-Nucleosomal Histone H3

Project description:Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here we characterize UBR7 as a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. UBR7 is a largely nuclear soluble protein. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. The pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3 nucleosomes in the absence of UBR7. We propose that the interaction of UBR7, NASP, and histones opposes the histone storage functions of NASP as UBR7 promotes reincorporation of post-nucleosomal H3 complexes.

2021-12-02 | GSE183730 | GEO

FBP1 expression in basal-like breast cancer MDA-MB231 and Hs578T cells

2012-09-27 | GSE41158 | GEO