Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cryptochromes-mediated Inhibition of the CRL4Cop1-Complex Assembly Defines an Evolutionary Conserved signaling mechanism

ABSTRACT: Cryptochromes-mediated Inhibition of the CRL4Cop1-Complex Assembly Defines an Evolutionary Conserved signaling mechanism

PROVIDER: PRJNA511889 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR8370440.fastq.gz	Fastqsanger.gz
	SRR8370450.fastq.gz	Fastqsanger.gz
	SRR8370460.fastq.gz	Fastqsanger.gz
	SRR8370470.fastq.gz	Fastqsanger.gz
	SRR8370480.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 72

Similar Datasets

Cryptochromes-mediated Inhibition of the CRL4Cop1-Complex Assembly Defines an Evolutionary Conserved signaling mechanism

Project description:Purpose: The goal of this study is to analyze the Cryptochrome-Cop1 axis in mammals Methods: mouse embryonic fibroblasts treated with dexamethasone, KL001 and/or Cop1 knockdown. Results: The transcriptomic analysis helps us to support our finding that the Cryptochromes-dependent repression of the glucocorticoid receptor is mediated by Cop1.

2019-05-01 | GSE124388 | GEO

Cryptochromes-Mediated Inhibition of the CRL4Cop1-Complex Assembly Defines an Evolutionary Conserved Signaling Mechanism.

Project description:In plants, cryptochromes are photoreceptors that negatively regulate the ubiquitin ligase CRL4Cop1. In mammals, cryptochromes are core components of the circadian clock and repressors of the glucocorticoid receptor (GR). Moreover, mammalian cryptochromes lost their ability to interact with Cop1, suggesting that they are unable to inhibit CRL4Cop1. Contrary to this assumption, we found that mammalian cryptochromes are also negative regulators of CRL4Cop1, and through this mechanism, they repress the GR transcriptional network both in cultured cells and in the mouse liver. Mechanistically, cryptochromes inactivate Cop1 by interacting with Det1, a subunit of the mammalian CRL4Cop1 complex that is not present in other CRL4s. Through this interaction, the ability of Cop1 to join the CRL4 complex is inhibited; therefore, its substrates accumulate. Thus, the interaction between cryptochromes and Det1 in mammals mirrors the interaction between cryptochromes and Cop1 in planta, pointing to a common ancestor in which the cryptochromes-Cop1 axis originated.

| S-EPMC6581574 | biostudies-literature

Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation

Project description:Cells rely on a diverse repertoire of genes for maintaining homeostasis, but the transcriptional networks underlying their expression remain poorly understood. The MOF acetyltransferase-containing Non-Specific Lethal (NSL) complex is a broad transcription regulator. It is essential in Drosophila and haploinsufficiency of the human KANSL1 subunit results in the Koolen-de Vries syndrome. Here, we perform a genome-wide RNAi screen and identify the BET protein BRD4 as evolutionary conserved co-factor of the NSL complex. Using Drosophila and mouse embryonic stem cells, we characterise a recruitment hierarchy, where NSL-deposited histone acetylation induces BRD4 recruitment for transcription of constitutively active genes. Transcriptome analyses in Koolen-de Vries patient-derived fibroblasts reveals perturbations with a cellular homeostasis signature that are evoked by the NSL complex/BRD4-axis. We propose that BRD4 represents a conserved bridge between the NSL complex and transcription activation and provide a new perspective in the understanding of their functions in healthy and diseased states.

2020-03-13 | GSE135815 | GEO

Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation

2020-03-13 | GSE135773 | GEO

Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation

2020-03-13 | GSE135772 | GEO

Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation

2020-03-13 | GSE135771 | GEO

Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation

Project description:Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation

| PRJNA560038 | ENA

Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation

Project description:Evolutionary conserved NSL complex/BRD4 axis controls transcription activation via histone acetylation