Phf23 regulates embryonic neurogenesis by increasing the level of H3K27ac of Tcf4 [CUT&Tag]
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ABSTRACT:
PROVIDER: PRJNA1163697 | ENA |
REPOSITORIES: ENA
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Project description:Epigenetic regulation is an important cell fate modality that is ubiquitous in neural development and plays an important role in both the fate determination and differentiation of neural stem cells (NSCs). The epigenetic regulator Phf23 is widely expressed in different human tissues and is involved in various biological processes, but its functional role in development has rarely been reported. Here, we found that Phf23 is an important epigenetic regulator that maintains embryonic neurogenesis in mice, and its absence leads to inhibition of the acetylation level of H3K27ac through the function of Hdac2, resulting in the blockage of embryonic NSCs differentiation at embryonic day 13.5 (E13.5). Tcf4, a transcription factor closely associated with neurogenesis, is a key downstream target gene of Phf23 in regulating embryonic neurogenesis, which may provide insights into the neuromodulatory network of the brain and the diagnosis and treatment of clinically relevant diseases.
2025-06-30 | GSE277737 | GEO
Project description:Epigenetic regulation is an important cell fate modality that is ubiquitous in neural development and plays an important role in both the fate determination and differentiation of neural stem cells (NSCs). The epigenetic regulator Phf23 is widely expressed in different human tissues and is involved in various biological processes, but its functional role in development has rarely been reported. Here, we found that Phf23 is an important epigenetic regulator that maintains embryonic neurogenesis in mice, and its absence leads to inhibition of the acetylation level of H3K27ac through the function of Hdac2, resulting in the blockage of embryonic NSCs differentiation at embryonic day 13.5 (E13.5). Tcf4, a transcription factor closely associated with neurogenesis, is a key downstream target gene of Phf23 in regulating embryonic neurogenesis, which may provide insights into the neuromodulatory network of the brain and the diagnosis and treatment of clinically relevant diseases.
2025-06-30 | GSE277736 | GEO
Project description:Phf23 regulates embryonic neurogenesis by increasing the level of H3K27ac of Tcf4 [RNA-seq]
| PRJNA1163696 | ENA
Project description:Genome binding/occupancy profiling of PHF23 and changes in H3K27ac based on the presence of PHF23
| PRJNA1279020 | ENA
Project description:Autophagy is a conserved self-digestion pathway essential for maintaining cellular homeostasis and catabolism. Under normal conditions, autophagic activity remains minimal but is rapidly upregulated in response to stresses such as nutrient deprivation. While the transcriptional and epigenetic activation of autophagy under nutrient deprived condition has been widely studied, less is known about the repression mechanisms of autophagy under normal conditions. Here, we identify PHF23 as an epigenetic repressor of autophagy through a CRISPR interference (CRISPRi) screening. PHF23 inhibits the expression of autophagy genes by recruiting the NuRD complex and reducing chromatin accessibility, particularly at enhancer regions. This repressive function of PHF23 requires an intact PHD domain and is attenuated under amino acid starvation or mTOR inhibition conditions. Notably, inhibiting PHF23 enhances the autophagic clearance of pathological protein aggregates including Tau and a1 antitrypsin Z variant (ATZ), underscoring its potential as a therapeutic target in diseases characterized by proteotoxic stress.
2025-12-17 | GSE300094 | GEO
Project description:PHF23 is a methyl reading protein with its PHD domain. We found PHF23 represses autophagy performed purification and identification of PHF23 interactome.
2025-12-15 | PXD065543 | Pride
Project description:We analyzed the genome wide localization of H3K4me3, H3K27me3 and the NUP98-PHF23 (with V5 tag) fusion protein which binds H3K4me3 via its PHD finger, using ChIP-seq. Results correlated with gene expression profiles. NUP98-PHF23 bound only 1.6% of H3K4me3 marks including Hoxa/b + Meis1. Assess H3K4me3 and H3K27me3 histone marks, and correlate these marks with chromatin binding of the NP23 fusion protein using lymphoblast and myeloblast cell lines derived from NP23 leukemias.
2014-03-06 | E-GEOD-54786 | biostudies-arrayexpress
Project description:We analyzed the genome wide localization of H3K4me3, H3K27me3 and the NUP98-PHF23 (with V5 tag) fusion protein which binds H3K4me3 via its PHD finger, using ChIP-seq. Results correlated with gene expression profiles. NUP98-PHF23 bound only 1.6% of H3K4me3 marks including Hoxa/b + Meis1.
2014-03-06 | GSE54786 | GEO
Project description:Autophagy is a conserved self-digestion pathway essential for maintaining cellular homeostasis and catabolism. Under normal conditions, autophagic activity remains minimal but is rapidly upregulated in response to stresses such as nutrient deprivation. While the transcriptional and epigenetic activation of autophagy under nutrient deprived condition has been widely studied, less is known about the repression mechanisms of autophagy under normal conditions. Here, we identify PHF23 as an epigenetic repressor of autophagy through a CRISPR interference (CRISPRi) screening. PHF23 inhibits the expression of autophagy genes by recruiting the NuRD complex and reducing chromatin accessibility, particularly at enhancer regions. This repressive function of PHF23 requires an intact PHD domain and is attenuated under amino acid starvation or mTOR inhibition conditions. Notably, inhibiting PHF23 enhances the autophagic clearance of pathological protein aggregates including Tau and a1 antitrypsin Z variant (ATZ), underscoring its potential as a therapeutic target in diseases characterized by proteotoxic stress.
2025-12-17 | GSE300095 | GEO
Project description:Autophagy is a conserved self-digestion pathway essential for maintaining cellular homeostasis and catabolism. Under normal conditions, autophagic activity remains minimal but is rapidly upregulated in response to stresses such as nutrient deprivation. While the transcriptional and epigenetic activation of autophagy under nutrient deprived condition has been widely studied, less is known about the repression mechanisms of autophagy under normal conditions. Here, we identify PHF23 as an epigenetic repressor of autophagy through a CRISPR interference (CRISPRi) screening. PHF23 inhibits the expression of autophagy genes by recruiting the NuRD complex and reducing chromatin accessibility, particularly at enhancer regions. This repressive function of PHF23 requires an intact PHD domain and is attenuated under amino acid starvation or mTOR inhibition conditions. Notably, inhibiting PHF23 enhances the autophagic clearance of pathological protein aggregates including Tau and a1 antitrypsin Z variant (ATZ), underscoring its potential as a therapeutic target in diseases characterized by proteotoxic stress.
2025-12-17 | GSE300092 | GEO