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Minor splicing factor 65K/RNPC3 interacts with ANKRD11 and mediates HDAC3-regulated histone deacetylation and transcription

ABSTRACT: Minor splicing factor 65K/RNPC3 interacts with ANKRD11 and mediates HDAC3-regulated histone deacetylation and transcription

PROVIDER: PRJNA1019690 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26140012_1.fastq.gz	Fastqsanger.gz
	SRR26140012_2.fastq.gz	Fastqsanger.gz
	SRR26140013_1.fastq.gz	Fastqsanger.gz
	SRR26140013_2.fastq.gz	Fastqsanger.gz
	SRR26140014_1.fastq.gz	Fastqsanger.gz

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Minor splicing factor 65K/RNPC3 interacts with ANKRD11 and mediates HDAC3-regulated histone deacetylation and transcription

Project description:Pre-mRNA splicing is coupled with DNA- and other RNA-processing machineries in the nucleus to form multilayer networks for accurate regulation of gene expression. However, those established couplings are major spliceosome-related, whether the minor spliceosome is involved remains unclear. Here, we first identified a direct interaction between a minor-specific protein 65K/RNPC3 and the histone deacetylase HDAC3 cofactor ANKRD11 through affinity co-purification using Drosophila lysate. In vivo assays revealed that the head of both DmAnkrd11Δ/Δ and Dm65KΔ/Δ mutants exhibited increased histone acetylation at H3K9 and H4K5, consistent with the high level of ANKRD11 in the central nervous systems. We then found that the 65K-ANKRD11 interaction is conserved in human, in which the HsANKRD11 middle-stretched domain mediates Hs65K association with HDAC3. CUT&Tag assays demonstrated that HDAC3 and Hs65K synergistically bind on chromatin, and the knockdown of ANKRD11 simultaneously decreased their bindings at the same chromatin locations and also increased nearby acetylation of H3K9. Sequencing of mRNAs revealed that the deficiency of HsANKRD11 or Hs65K caused changes in gene expression correlated with their chromatin-binding changes of HDAC3 and Hs65K and the levels of H3K9ac. This study provides a novel strategy for the regulation of histone deacetylation and gene expression through a minor spliceosome-specific component.

2024-03-31 | GSE243715 | GEO

Minor Spliceosomal 65K/RNPC3 Interacts with ANKRD11 and Mediates HDAC3-Regulated Histone Deacetylation and Transcription.

Project description: Not available

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CPSF6-RARγ Interacts with HDAC3 to Promote Myeloid Transformation

Project description:CPSF6-RARγ Interacts with HDAC3 to Promote Myeloid Transformation

| PRJNA1026639 | ENA

CPSF6-RARγ Interacts with HDAC3 to Promote Myeloid Transformation [RNA-seq]

Project description:CPSF6-RARγ Interacts with HDAC3 to Promote Myeloid Transformation [RNA-seq]

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Ankrd11 deficiency reverses the dysfunction of chronic HBV-specific T-cell [RNA-seq]

Project description:To investigate the transcriptomic changes in CD8 T cells upon Ankrd11 deficiency, we performed RNA-seq to analyze alterations in the transcriptome between Ankrd11-knockout and wild-type CD8 T cells.

2026-07-25 | GSE299520 | GEO

Ankrd11 deficiency reverses the dysfunction of chronic HBV-specific T-cell [Cut&Tag]

Project description:To investigate the impact of Ankrd11 deficiency on H3K27ac modification in CD8 T cells, we performed H3K27ac CUT&Tag assays comparing H3K27ac modification levels between Ankrd11-knockout and wild-type CD8 T cells.

2026-07-25 | GSE299521 | GEO

Ankrd11 deficiency reverses the dysfunction of chronic HBV-specific T-cell [ATAC-seq]

Project description:To investigate the impact of Ankrd11 deficiency on chromatin accessibility in CD8 T cells, we performed ATAC-seq to analyze differences in chromatin openness between Ankrd11-knockout CD8 T cells and wild-type CD8 T cells.

2026-07-25 | GSE299519 | GEO

RNA-Seq of SETD5 W834C and ANKRD11 E2522K homozygous mESCs with matched controls

Project description:Setd5 and Ankrd11 are components of the mammalian SET3C complex which are mutated in neuro developmental disorders. We have generated independent clones of mESCs with a missense mutation equivalent to the KBG syndrome mutation E2522K in Ankrd11. We have also generated independent clones of mESCs with W834C and ΔKWK (where K833 to K835 are missing) in Setd5.

2026-04-27 | E-MTAB-15318 | biostudies-arrayexpress

Expression data from Ankrd11Yod/+ and WT embryonic cortical neurospheres

Project description:Ankrd11 is a potential chromatin regulator implicated in neural development and autism spectrum disorder (ASD) with no known function in the brain. Here, we show that knockdown of Ankrd11 in developing murine or human cortical neural precursors caused decreased proliferation, reduced neurogenesis, and aberrant neuronal positioning. Similar cellular phenotypes and aberrant ASD-like behaviors were observed in Yoda mice carrying a point mutation in the Ankrd11 HDAC-binding domain. Consistent with a role for Ankrd11 in histone acetylation, Ankrd11 was associated with chromatin, colocalized with HDAC3, and expression and histone acetylation of Ankrd11 target genes were altered in Yoda neural precursors. Moreover, the Ankrd11 knockdown-mediated decrease in precursor proliferation was rescued by inhibiting histone acetyltransferase activity or expressing HDAC3. Thus, Ankrd11 is a crucial epigenetic regulator of neural development that controls histone acetylation and gene expression, thereby providing a likely explanation for its association with cognitive dysfunction and ASD. We used microarrays to compare the gene expression profile in embryonic neurospheres prepared from neocortices of WT and Ankrd11Yod/+ mice E14.5 cortical secondary neurosheres 5 days post-passage were collected and total RNA extracted. cDNA was hybridized on Affymetrix Mouse Gene 2.0 ST Array and gene expression was analyzed using Parterk software. In total, 6 Ankrd11Yod/+ and 5 WT embryos were used.

2014-11-15 | E-GEOD-63303 | biostudies-arrayexpress

Nuclear Receptor Corepressors are Required for the Histone Deacetylase Activity of HDAC3 In Vivo

Project description:Histone deacetylase 3 (HDAC3) is an epigenome-modifying enzyme that is required for normal mouse development and tissue-specific functions. In vitro, HDAC3 protein itself has minimal enzyme activity, but gains its histone deacetylation function from stable association with the conserved deacetylase activation domain (DAD) contained in nuclear receptor corepressors NCOR1 and SMRT. Here we show that HDAC3 enzyme activity is undetectable in mice bearing point mutations in the DAD of both NCOR1 and SMRT (NS-DADm), despite normal levels of HDAC3 protein. Local histone acetylation is increased, and genomic HDAC3 recruitment is reduced though not abrogated. Remarkably, the NS-DADm mice are born and live to adulthood, whereas genetic deletion of HDAC3 is embryonic lethal. These findings demonstrate that nuclear receptor corepressors are required for HDAC3 enzyme activity in vivo, and suggest that a deacetylase-independent function of HDAC3 may be required for life. This SuperSeries is composed of the SubSeries listed below. Refer to individual Series.

2013-01-01 | E-GEOD-42541 | biostudies-arrayexpress

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