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LATS kinase-mediated selective disruption of CTCF genomic binding

ABSTRACT: LATS kinase-mediated selective disruption of CTCF genomic binding

PROVIDER: PRJNA470938 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7146386.fastq.gz	Fastqsanger.gz
	SRR7146387.fastq.gz	Fastqsanger.gz
	SRR8928700.fastq.gz	Fastqsanger.gz
	SRR8928700_1.fastq.gz	Fastqsanger.gz
	SRR8928700_2.fastq.gz	Fastqsanger.gz

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LATS kinase-mediated selective disruption of CTCF genomic binding

Project description:We identified CTCF as a substrate of the LATS kinases. Under cellular stress conditions that activated LATS, CTCF was phosphorylated in a LATS-dependent manner and lost DNA-binding activity. LATS signaling target genes resided in CTCF-mediated insulated neighborhoods and depended on such chromatin organization to sustain their expression. Genome-wide CTCF DNA-binding profiling revealed that metabolic stress reduced CTCF occupancy specifically at a small subset of CTCF-binding sites that encompassed many LATS target genes and were most significantly associated with LATS signaling. Dissociation of CTCF from LATS target genes disrupted corresponding CTCF-mediated chromatin domains and downregulated LATS target gene expression.

2020-03-09 | GSE114319 | GEO

Genetic disruption of Ctcf destabilizes DNA methylation

Project description:Ctcf heterozygous knockout mice are susceptible to neoplasia in a broad range of tissues, including lymphoma, endometrial cancer, and non-small cell lung cancer. Retention of the wild type Ctcf allele in these tumors establishes CTCF as a haploinsufficient tumor suppressor gene. Both human tumors and normal murine tissues with CTCF disruption are characterized by genome-wide differences in DNA methylation relative to CTCF wild type tissues, indicating even modest disruption of CTCF broadly destabilizes DNA methylation in vivo. This cross species functional analysis identifies CTCF as a commonly mutated tumor suppressor gene and establishes a central role for DNA methylation stability in tumor suppression. RRBS sequencing of transgenic Ctcf heterozygous mice and wild-type litter mate whole lung tissue.

2014-07-30 | E-GEOD-48975 | biostudies-arrayexpress

LATS kinase-mediated CTCF phosphorylation and selective loss of genomic binding.

Project description:Chromatin topological organization is instrumental in gene transcription. Gene-enhancer interactions are accommodated in the same CTCF-mediated insulated neighborhoods. However, it remains poorly understood whether and how the 3D genome architecture is dynamically restructured by external signals. Here, we report that LATS kinases phosphorylated CTCF in the zinc finger (ZF) linkers and disabled its DNA-binding activity. Cellular stress induced LATS nuclear translocation and CTCF ZF linker phosphorylation, and altered the landscape of CTCF genomic binding partly by dissociating it selectively from a small subset of its genomic binding sites. These sites were highly enriched for the boundaries of chromatin domains containing LATS signaling target genes. The stress-induced CTCF phosphorylation and locus-specific dissociation from DNA were LATS-dependent. Loss of CTCF binding disrupted local chromatin domains and down-regulated genes located within them. The study suggests that external signals may rapidly modulate the 3D genome by affecting CTCF genomic binding through ZF linker phosphorylation.

| S-EPMC7030924 | biostudies-literature

Selective Disruption of Core Regulatory Transcription

Project description:Selective Disruption of Core Regulatory Transcription

| PRJNA494422 | ENA

Genetic disruption of Ctcf destabilizes DNA methylation

2014-07-30 | GSE48975 | GEO

Fission yeast NDR/LATS kinase Orb6 regulates exocytosis via phosphorylation of exocyst complex

Project description:NDR/LATS kinases regulate multiple aspects of cell polarity and morphogenesis from yeast to mammals, but few of their substrates are known. Fission yeast NDR/LATS kinase Orb6 has been proposed to control cell polarity via spatial regulation of Gef1, a guanine nucleotide exchange factor for the small GTPase Cdc42. Here we show that Orb6 plays a critical role as a positive regulator of exocytosis, independent of Gef1. Through Orb6 inhibition in vivo and quantitative global phosphoproteomics, we identify several proteins involved in membrane trafficking as Orb6 targets, and we confirm Sec3 and Sec5, conserved components of the exocyst complex, as substrates of Orb6 both in vivo and in vitro. Our results suggest that Orb6 kinase activity is crucial for exocyst localization to actively-growing cell tips and for exocyst activity during septum dissolution after cytokinesis. We further show that Orb6 phosphorylation of Sec3 serine-201 contributes to exocyst function in parallel with exocyst protein Exo70. We propose that Orb6 contributes to polarized growth by regulating membrane trafficking at multiple levels.

2019-01-31 | PXD009408 | Pride

Selective Disruption of Core Regulatory Transcription [ChIP-seq]

Project description:Selective Disruption of Core Regulatory Transcription [ChIP-seq]

| PRJNA478223 | ENA

Selective Disruption of Core Regulatory Transcription [AQuA-HiChIP]

Project description:Selective Disruption of Core Regulatory Transcription [AQuA-HiChIP]

| PRJNA494423 | ENA

Selective Disruption of Core Regulatory Transcription [RNA-seq]

Project description:Selective Disruption of Core Regulatory Transcription [RNA-seq]

| PRJNA495665 | ENA

LATS regulates heavy metal response

Project description:LATS regulates heavy metal response