Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer

ABSTRACT: The forkhead protein FOXA1 has been found to play a critical role in orchestrating hormonal-signaling network and to function as a pioneer factor to regulate breast-specific gene expression,However, whether interplay between O-GlcNAcylation and FOXA1 affects the genome-wide transcriptional activity of this TF and subsequently orchestrates downstream gene expression networks in breast cancer progression needs further elucidation.

ORGANISM(S): Homo Sapiens

SUBMITTER: Yubo Liu

PROVIDER: PXD039019 | iProX | Wed Dec 21 00:00:00 GMT 2022

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Publications

FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer.

Liu Yajie Y Yu Kairan K Kong Xiaotian X Zhang Keren K Wang Lingyan L Zhang Nana N Chen Qiushi Q Niu Mingshan M Li Wenli W Zhong Xiaomin X Wu Sijin S Zhang Jianing J Liu Yubo Y

Science advances 20230818 33

FOXA1, a transcription factor involved in epigenetic reprogramming, is crucial for breast cancer progression. However, the mechanisms by which FOXA1 achieves its oncogenic functions remain elusive. Here, we demonstrate that the O-linked β-N-acetylglucosamine modification (O-GlcNAcylation) of FOXA1 promotes breast cancer metastasis by orchestrating the transcription of numerous metastasis regulators. O-GlcNAcylation at Thr432, Ser441, and Ser443 regulates t ...[more]

PMID: 37595040

Similar Datasets

FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer [ChIP-seq]

Project description:The transcription factor FOXA1, which functions in epigenetic reprogramming, plays a critical role in breast cancer progression. However, the molecular mechanisms by which FOXA1 achieves its oncogenic functions remain elusive. Here, we demonstrate that the O-GlcNAcylation of FOXA1 increases breast cancer metastasis capacity by orchestrating the transcription of numerous metastasis regulators. O-GlcNAcylation at Thr432, Ser441 and Ser443 regulates the stability of FOXA1 and promotes its assembly with chromatin in breast cancer cells. We provide evidence that O-GlcNAcylation shapes the FOXA1 interactome, especially triggering the recruitment of the transcriptional repressor MECP2 and consequently stimulating FOXA1 chromatin-binding sites to switch to chromatin loci of adhesion-related genes, including EPB41L3 and COL9A2. Site-specific depletion of O-GlcNAcylation on FOXA1 affects the expression of various downstream genes and thus inhibits breast cancer proliferation and metastasis both in vitro and in vivo.

2023-01-02 | GSE221933 | GEO

FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer [RNA-seq]

2023-01-02 | GSE221934 | GEO

GlcNAcylation of histone H2B facilitates its monoubiquitination

Project description:This SuperSeries is composed of the following subset Series: GSE33049: GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data] GSE33050: GlcNAcylation of histone H2B facilitates its monoubiquitination [Affymetrix data] Refer to individual Series

2011-10-26 | E-GEOD-33051 | biostudies-arrayexpress

GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

Project description:We report that histone GlcNAcylation of H2B S112 is a vital histone modification which facilitates histone monoubiquitination (ub). In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over entire chromosomes including transcribed gene loci, together with co-localization of H2B S112 GlcNAcylation and K120 ub. Examination of H2B S112 GlcNAc and H2B K120 ub in HeLa S3 cells

2011-10-27 | E-GEOD-33049 | biostudies-arrayexpress

GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

2011-10-27 | GSE33049 | GEO

Temporal regulation of Lsp1 O-GlcNAcylation and phosphorylation duringactivated Bcellsapoptosis

Project description:Here, we decipher the molecular mechanisms bridging B cell activation and apoptosis mediated by post-translational modification(PTM). We found that O-GlcNAcase inhibition enhances B cell activation and apoptosisinduced by B cell receptor (BCR)cross-linking. This proteome-scale analysis of the functional interplay between protein O-GlcNAcylation and phosphorylation in stimulated mouse primary B cells identified313O-GlcNAcylation-dependent phosphositeson 224 phosphoproteins.Among these phosphoproteins, temporal regulation ofthe O-GlcNAcylation and phosphorylation of lymphocyte-specific protein-1 (Lsp1) is a key switch that triggersapoptosis in activated B cells. O-GlcNAcylation at S209 of Lsp1, identified as the major O-GlcNAc site on Lsp1 by both electron-transfer dissociationand collision-induced dissociationtandem mass spectrometry,was a prerequisite for the recruitment of its kinase, PKC-β1, to induce S243 phosphorylation, leading to ERK activation and down-regulation of BCL-2 and BCL-xL. Thus, we demonstrate the critical PTM interplay of Lsp1 that transmits signals for initiating apoptosis after BCR ligation.

2016-09-26 | PXD003788 | Pride

O-GlcNAcylation elevates topoisomerase IIα catalytic activity: a role in the chemotherapy resistance of breast cancer

Project description:DNA topoisomerase IIα (TOP2A) plays a vital role in replication and cell division by catalytically altering DNA topology. It is a prominent target for anticancer drugs. However, it is currently unknown whether TOP2A is O-GlcNAc-modified, and the mechanism by which interplay between TOP2A and O-GlcNAcylation affects breast cancer chemotherapeutic drug resistance remains unclear.

2023-03-31 | PXD041284 |

Inhibition of O-GlcNAcylation via O-GlcNAc transferase fosters megakaryopoiesis and induces thrombopoiesis

Project description:We report that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs) and that inhibition of O-GlcNAc transferase (OGT), of which catalyzes O-GlcNAcylation, prolongedly decreases O-GlcNAcylation and induces megakaryopoiesis and thrombopoiesis. To gain the better insight into the potential mechanisms underlying platelet regulation by O-GlcNAcylation ,we compared the genome-wide transcription profiles of megakaryblastic MEG-01 cells with decreased O-GlcNAcylation (OGTi) and its control counterpart using RNA sequencing. Gene ontology and enrichment analysis of differentially expressed genes suggest that platelet formation might be regulated through the perturbation in cell adhesion molecules, i.e. integrin-a4 and b7, downstream of O-GlcNAc/c-Myc axis.

2020-08-06 | GSE150880 | GEO

FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer.

Project description:FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer.

| PRJNA916875 | ENA

O-GlcNAcylation Mediates Wnt-stimulated Bone Formation via Rewiring Aerobic Glycolysis in Osteoblast-lineage Cells

Project description:As the efficient therapeutic treatment for osteoporosis, Wnt signaling is considered to induce bone formation through aerobic glycolysis. However, the mechanism underlying the regulatory role of Wnt in orchestrating glucose metabolism during osteogenesis remains unclear. O-GlcNAcylation, a dynamic posttranslational modification (PTM) on proteins, controls multiple critical biological processes including gene transcription, translation, and cell fate determination. Here, we report Wnt3a either induces O-GlcNAcylation rapidly via the Ca2+-PKA-Gfat1 axis, or increases it in a Wnt-β-catenin dependent manner during prolonged stimulation. Importantly, O-GlcNAcylation is found indispensable for osteoblastogenesis both in vivo and in vitro. Genetic ablation of O-GlcNAcylation in osteoblast-lineage cells diminishes bone formation and delays bone fracture healing in response to Wnt stimulation. Notably, Wnt3a-induced O-GlcNAcylation enhances aerobic glycolysis by stabilizing PDK1 partially through Serine 174 (S174) site, which consequently facilitates osteogenesis. These findings highlight that O-GlcNAcylation is indispensable in Wnt-induced glucose metabolism during osteogenesis, indicating its potential as a therapeutic target for osteoporosis.

2024-06-28 | GSE251951 | 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