BRD9-mediated control of the TGF-β/Activin/Nodal pathway regulates self-renewal and differentiation of human embryonic stem cells and progression of cancer cells.
Xuepeng WangChengcheng SongYing YeYashi GuXuemei LiPeixin ChenDongliang LengJing XiaoHao WuSisi XieWeiwei LiuQi ZhaoDi ChenXi ChenQiang WuGuokai ChenWensheng ZhangPublished in: Nucleic acids research (2023)
Bromodomain-containing protein 9 (BRD9) is a specific subunit of the non-canonical SWI/SNF (ncBAF) chromatin-remodeling complex, whose function in human embryonic stem cells (hESCs) remains unclear. Here, we demonstrate that impaired BRD9 function reduces the self-renewal capacity of hESCs and alters their differentiation potential. Specifically, BRD9 depletion inhibits meso-endoderm differentiation while promoting neural ectoderm differentiation. Notably, supplementation of NODAL, TGF-β, Activin A or WNT3A rescues the differentiation defects caused by BRD9 loss. Mechanistically, BRD9 forms a complex with BRD4, SMAD2/3, β-CATENIN and P300, which regulates the expression of pluripotency genes and the activity of TGF-β/Nodal/Activin and Wnt signaling pathways. This is achieved by regulating the deposition of H3K27ac on associated genes, thus maintaining and directing hESC differentiation. BRD9-mediated regulation of the TGF-β/Activin/Nodal pathway is also demonstrated in the development of pancreatic and breast cancer cells. In summary, our study highlights the crucial role of BRD9 in the regulation of hESC self-renewal and differentiation, as well as its participation in the progression of pancreatic and breast cancers.
Keyphrases
- embryonic stem cells
- transforming growth factor
- endothelial cells
- lymph node
- epithelial mesenchymal transition
- cell proliferation
- genome wide
- breast cancer cells
- neoadjuvant chemotherapy
- squamous cell carcinoma
- gene expression
- signaling pathway
- dna damage
- physical activity
- mouse model
- risk assessment
- young adults
- oxidative stress
- small molecule
- climate change
- long non coding rna
- amino acid
- binding protein
- dna methylation
- locally advanced