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Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [RNA-Seq]

ABSTRACT: Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [RNA-Seq]

PROVIDER: PRJNA542336 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR9041012.fastq.gz	Fastqsanger.gz
	SRR9041013.fastq.gz	Fastqsanger.gz
	SRR9041014.fastq.gz	Fastqsanger.gz
	SRR9041015.fastq.gz	Fastqsanger.gz
	SRR9041016.fastq.gz	Fastqsanger.gz

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Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling

Project description:Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling

| PRJNA542332 | ENA

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [ChIP-Seq]

Project description:Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [ChIP-Seq]

| PRJNA542334 | ENA

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [HeLa ATAC-Seq]

Project description:Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [HeLa ATAC-Seq]

| PRJNA542333 | ENA

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [U2OS ATAC-Seq]

Project description:Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [U2OS ATAC-Seq]

| PRJNA542335 | ENA

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [ChIP-Seq]

Project description:The Tousled like kinases 1 and 2 (TLK1/2) control histone deposition through the ASF1 histone chaperones and are regulated by the DNA damage response. Depletion of TLK activity caused replication stress, increased chromosomal instability and cell arrest or death. Here, we show that stalled forks in TLK depleted cells are processed by BLM, SAMHD1 and the MRE11 nuclease to generate ssDNA and activate checkpoint signaling. TLK depletion also impaired heterochromatin maintenance, inducing features of alternative lengthening of telomeres and increasing spurious expression of other repetitive elements, associated with impaired deposition of the histone variant H3.3. TLK depletion culminated in a BLM-dependent, STING-mediated innate immune response. In many human cancers, TLK1/2 expression correlated with signatures of chromosomal instability and anti-correlated with STING and innate and adaptive immune response signatures. Together, our results show that TLK activity protects replication forks from active processing, contributes to chromatin silencing and suppresses innate immune responses, suggesting that TLK amplification may protect chromosomally unstable cancers from immune detection.

2020-07-21 | GSE131021 | GEO

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [RNA-Seq]

2020-07-21 | GSE131019 | GEO

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [HeLa ATAC-Seq]

2020-07-21 | GSE131022 | GEO

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling [U2OS ATAC-Seq]

2020-07-21 | GSE131020 | GEO

Tousled-like kinase activity is required for transcriptional silencing and suppression of innate immune signaling

Project description:This SuperSeries is composed of the SubSeries listed below.

2020-07-21 | GSE131023 | GEO

Molecular basis of Tousled-Like-Kinase 2 (TLK2) activation – LC-MS/MS-based analysis of TLK2 phosphorylation state

Project description:In this study on human Tousled-Like-Kinase 2 (TLK2) mass spectrometry-based analysis was applied as part of a molecular characterization of TLK2 in the aim to increase the understanding of the mode of activation of this protein. Specifically, different TLK2 constructs were analyzed to generate a “phosphorylation map” of the TLK2 protein. To analyse the phosphorylation state of TLK2 we used recombinant protein purified from Escherichia coli. Samples of different TLK2 constructs were used for in-gel digestion and analysed by mass spectrometry. All samples were prepared and run in triplicates for label-free quantification. Explanation for MS raw files with TLK2 construct included: Ac: TLK2 construct consisting of amino acid residues 191-772 (Ac indicates active form). KD: TLK2 construct consisting of amino acid residues 191-772 with mutation D613A (KD indicates kinase-dead form). FusionKD: Kinase-dead part of a heterodimeric TLK2 construct (amino acid residues 191-772) with mutation D613A (KD indicates kinase-dead form). FusionAC: Active part of a heterodimeric TLK2 construct (amino acid residues 191-772) (Ac indicates kinase-dead form). KDlong: Kinase domain of TLK2 with C-tail (amino acid residues 450-772). KDshort: Kinase domain of TLK2 without C-tail (amino acid residues 450-753).

2018-10-23 | PXD007675 | Pride

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