Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [RNA-Seq]

ABSTRACT: FOXA1 transcription factor is essential for the development and maturation of prostate luminal epithelial cells. FOXA1 gene is frequently mutated and its expression is deregulated during prostate cancer progression. We and others have shown that FOXA1 induces androgen-dependent cell growth by transcriptional regulation of target genes related to cell cycle process, DNA replication, cell division, and apoptosis. Despite of its important roles, how FOXA1 expression itself is regulated in prostate cancer cells remains largely unknown. Here we report that EZH2 methylates one of the lysine residues (K295) on FOXA1 protein to reduce its ubiquitination and subsequent degradation. Mechanistically, this EZH2-mediated FOXA1 methylation recruits BUB3/USP7 deubiquitinase complex to remove FOXA1 ubiquitination for increased protein stability.

ORGANISM(S): Homo sapiens

PROVIDER: GSE161518 | GEO | 2021/04/15

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [ChIP-Seq]

Project description:FOXA1 transcription factor is essential for the development and maturation of prostate luminal epithelial cells. FOXA1 gene is frequently mutated and its expression is deregulated during prostate cancer progression. We and others have shown that FOXA1 induces androgen-dependent cell growth by transcriptional regulation of target genes related to cell cycle process, DNA replication, cell division, and apoptosis. Despite of its important roles, how FOXA1 expression itself is regulated in prostate cancer cells remains largely unknown. Here we report that EZH2 methylates one of the lysine residues (K295) on FOXA1 protein to reduce its ubiquitination and subsequent degradation. Mechanistically, this EZH2-mediated FOXA1 methylation recruits BUB3/USP7 deubiquitinase complex to remove FOXA1 ubiquitination for increased protein stability.

2021-04-15 | GSE161517 | GEO

Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer

Project description:Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer

| PRJNA678634 | ENA

Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [RNA-Seq]

Project description:Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [RNA-Seq]

| PRJNA678636 | ENA

Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [ChIP-Seq]

Project description:Regulation of FOXA1 protein stability by Polycomb and BUB3/USP7 deubiquitin complexes in prostate cancer [ChIP-Seq]

| PRJNA678635 | ENA

YG001: A Usp7-Tip60 pathway regulates early adipogenesis

Project description:USP7, a dominant DUB activity in 3T3-L1 adipocytes and in mouse adipose tissue, increases Tip60 protein levels, and deubiquitinates Tip60 both in intact cells and in vitro. Treatment with a pan deubiquitinase (DUB) inhibitor, or knockdown of USP7, decreases adipogenesis. Transcriptome analysis reveals a common set of cell cycle genes to be co-regulated by both Tip60 and USP7. Knock down of either factor results in impaired mitotic clonal expansion, an early step in adipogenesis. These results therefore reveal deubiquitination of a transcriptional coregulator to be a key mechanism in the regulation of early adipogenesis Mature 3T3-L1 adipocytes were subjected to RNAi-mediated knock down with control(C), USP7(U)- or Tip60(T)-specific oligonucleotides. For this, 4 replicates of differentiated 3T3-L1 cells were transfected with Amaxa technology. Two days after transfection cells were washed twice with PBS twice and lysed in 0.5ml Trizol (Invitrogen). mRNA expression of Tip60 and USP7 was assessed by qRT-PCR. Amplified cRNA samples were labeled with either cy3 or cy5 and put on microarray together with and oppositely labeled common reference sample consisting of cRNA derived from undifferentiated 3T3-L1 cells.

2013-08-28 | E-GEOD-28587 | biostudies-arrayexpress

Expression analysis of knockdown of USP7 in HEK293T cells.

Project description:Ubiquitin Specific Peptidase 7 (USP7) is a deubiquitinase of several important regulatory proteins, and important regulator of TGFb pathway. To investigate their role in cell signaling, we analyzed global mRNA levels in HEK293T cells that were knocked down with shRNAs against USP7 and non-targeting control (CTRL).

2020-10-18 | GSE139094 | GEO

Genome-wide maps of chromatin state in A375 cells or in normal or USP7 knockdown A375 cells .

Project description:ChIP-seq experiments were performed in normal or USP7 knockdown A375 cells with specific antibodies against USP7, EZH2, H3K27me3 and H2BK120ub1. Consistent with our expectations, the analysis of ChIP-seq data showed that USP7 loss-of-function led to obviously reduction in USP7, EZH2 and H3K27me3 around the USP7-specific peaks, but an upregulation in H2BK120ub1. This study gave us a new understanding that USP7 is required for EZH2 loading and H3K27 trimethylation.

2020-05-01 | GSE133834 | GEO

YG001: A Usp7-Tip60 pathway regulates early adipogenesis

2013-08-28 | GSE28587 | GEO

Effect of the USP7 inhibitor HBX41,108 on lipopolysaccharide induced gene expression in mouse bone marrow derived macrophages.

Project description:USP7 is a deubiquitinase enzyme that removes polyubiquitin chains form a number of substrates including MDM2, p53 and NF-κB. In this study we assessed the impact of the USP7 inhibitor HBX41,108 on lipopolysaccharide (LPS) induded transcriptional responses in murine bone marrow derived macrophages.

2020-06-15 | GSE149478 | GEO

USP7 protects TFEB from proteasome-mediated degradation

Project description:The transcription factor EB (TFEB) is a master regulator of lysosomal biogenesis and autophagy. We identify a distinct nuclear interactome of TFEB, with USP7 emerging as a key post-translational modulator of TFEB. Genetic depletion and inhibition of USP7 reveal its critical role in preserving TFEB stability within both nuclear and cytoplasmic compartments. Specifically, USP7 is identified as the deubiquitinase responsible for removing the K48-linked polyubiquitination signal from TFEB at lysine residues K116, K264, and K274, thereby preventing its proteasomal degradation. Functional assays demonstrate the involvement of USP7 in preserving TFEB-mediated transcriptional responses to nutrient deprivation, while also modulating autophagy flux and lysosome biogenesis. As USP7 is a deubiquitinase that protects TFEB from proteasomal degradation, these findings provide the foundation for therapeutic targeting of the USP7-TFEB axis in conditions characterized by TFEB dysregulation and metabolic abnormalities, particularly in certain cancers.

2024-09-17 | PXD055937 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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