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Androgen receptor requires an optimal level of condensation to assemble androgen-induced active enhancers [ChIP-Seq]

ABSTRACT: Androgen receptor requires an optimal level of condensation to assemble androgen-induced active enhancers [ChIP-Seq]

PROVIDER: PRJNA889015 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21853551.fastq.gz	Fastqsanger.gz
	SRR21853552.fastq.gz	Fastqsanger.gz
	SRR21853553.fastq.gz	Fastqsanger.gz
	SRR21853554.fastq.gz	Fastqsanger.gz
	SRR21853555.fastq.gz	Fastqsanger.gz

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Androgen receptor requires an optimal level of condensation to assemble androgen-induced active enhancers [GRO-Seq]

Project description:Androgen receptor requires an optimal level of condensation to assemble androgen-induced active enhancers [GRO-Seq]

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Androgen receptor requires an optimal level of condensation to assemble androgen-induced active enhancers [GRO-Seq]

Project description:Transcription factors (TFs) activate enhancers to drive cell-specific gene expression in response to signals, but our understanding of enhancer assembly in signaling events is incomplete. Here we show that Androgen Receptor (AR), a steroid hormone signaling-regulated transcription factor, forms phase-separated condensates in response to androgen to activate enhancers. We demonstrate that the intrinsically disordered NTD of AR drives condensate formation and that NTD deletion or aromatic residue mutation reduces AR self-association and abolishes AR transcriptional activity. AR NTD can be substituted by some IDRs from other proteins for AR condensation capacity and transactivation function. Extending the polyQ tract within AR NTD strengthens AR phase separation and also leads to impaired transcriptional activity. PolyQ expansion does not affect AR binding on enhancers, but instead impairs enhancer assembly. These results suggest that AR phase separation mediates enhancer assembly, and an optimal level of AR condensation is required for its proper function in mediating AR-AR homotypic and AR-cofactor heterotypic interactions to regulate transcription in response to signals. Our study supports that alteration of the fine-tuned protein condensation might underlie AR-related human pathologies, therefore providing novel molecular insights for potential therapeutic strategies to treat prostate cancer and other AR-involved diseases by targeting AR condensation.

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Androgen receptor requires an optimal level of condensation to assemble androgen-induced active enhancers [ChIP-Seq]

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Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions

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Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions

Project description:Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions

| PRJNA889016 | ENA

Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions

Project description:Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions

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Vascularized And Complex Organ Buds From Diverse Tissues Via Mesenchymal Cell-Driven Condensation

Project description:Here, we demonstrate a generalized method for organ bud formation from diverse tissues by combining pluripotent stem cell-derived tissue-specific progenitors or relevant tissue samples with endothelial cells and mesenchymal stem cells (MSCs). The MSCs initiated condensation within these heterotypic cell mixtures, which was dependent upon substrate matrix stiffness. Defining optimal mechanical properties promoted formation of 3D, transplantable organ buds from tissues including kidney, pancreas, intestine, heart, lung, and brain. Transplanted pancreatic and renal buds were rapidly vascularized and self-organized into functional, tissue-specific structures. These findings provide a general platform for harnessing mechanical properties to generate vascularized, complex organ buds with broad applications for regenerative medicine. Gene expression profiles of development-related gene expression in kidney bud transplants and murine kidneys.

2015-07-01 | E-GEOD-66454 | biostudies-arrayexpress

The Histone Variant H2A.W Defines Heterochromatin and Promotes Chromatin Condensation in Arabidopsis

Project description:Histone variants play crucial roles in gene expression, genome integrity and chromosome segregation. However, to what extent histone variants control chromatin architecture remains largely unknown. Here, we show that the previously uncharacterized histone variant H2A.W plays a crucial role in condensation of heterochromatin. Genome-wide profiling of all four types of H2A variants in Arabidopsis shows that H2A.W specifically associates with heterochromatin. H2A.W recruitment is independent of heterochromatic marks H3K9me2 and DNA methylation. Genetic interactions show that H2A.W acts in synergy with CMT3 mediated methylation to maintain genome integrity. In vitro, H2A.W enhances chromatin condensation through a higher propensity to make fiber-to-fiber interactions via its conserved C-terminal motif. In vivo, elimination of H2A.W causes decondensation of heterochromatin and conversely, ectopic expression of H2A.W promotes heterochromatin condensation. These results demonstrate that H2A.W plays critical roles in heterochromatin by promoting higher order chromatin condensation. Since similar H2A.W C-terminal motifs are present in other variant found in mammals and other organisms our findings impact our understanding of heterochromatin condensation in a wide variety of eukaryotic organisms. Two mRNA-seq samples, two bisulfite-seq samples, six ChIP-seq samples.

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