Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ATR phosphoproteomics - substrate validation

ABSTRACT: ATR phosphoproteomics - Validation of ATR substrates as identified in phosphoproteomics screen. Sample Processing Protocol: Samples were processed as detailed in the accompanying manuscript. Data Processing Protol: Data were processed as detailed in the accompanying manuscript and the attached R script files.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Rouse

PROVIDER: PXD040476 | JPOST Repository | Tue Jan 16 00:00:00 GMT 2024

REPOSITORIES: jPOST

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	ATR_TMT_Validation_R-scripts.zip	Other
	LUM190801-10_FW052_S-01_FW.raw	Raw
	LUM190801-16_FW052_TL-01_FW.raw	Raw
	MQ_params_ATR_validation.xml	Xml
	evidence.txt	Txt

Items per page:

1 - 5 of 5

Similar Datasets

ATR phosphoproteomics screening using berzosertib and gartisertib

Project description:ATR phosphoproteomics screening using berzosertib and gartisertib Quantitiative phosphoproteomics using TMT10plex labelling and basic reverse phase HPLC prefractionation. Experimental and data analysis procedures detailed in the accompanying manuscript. Data analysis scripts included in this submission.

2024-01-15 | PXD040469 | JPOST Repository

Genome-wide fork-collapse sites in MEFs from ATR inhibition [mouse]

Project description:Transient obstruction of DNA polymerase progression activates the ATR checkpoint kinase, which suppresses fork breakage, strand resection, and RPA accumulation. Herein, we use a developed DNA break-detection assay, BrITL, to identify replication-problematic loci (RPLs) that become processed into persistent double-strand breaks across the mammalian genome from ATR inhibition.

2018-10-04 | GSE115624 | GEO

ATR - phosphoproteomics - DHX9 validation HEK293

Project description:Validation of the phosphorylation of S321 in DHX9 by ATR. Samples: (A): Hydroxyurea + ATR inhibitor treated; (C) Hydroxyurea + Chk1 inhibitor treated; (H): Hydroxyurea treated.

2024-04-11 | PXD050954 | JPOST Repository

ATR - phosphoproteomics - DHX9 validation HeLa

2024-04-11 | PXD050953 | JPOST Repository

Genome-wide fork-collapse sites in MDA-MB-231 cells from ATR inhibition [human]

Project description:Transient obstruction of DNA polymerase progression activates the ATR checkpoint kinase, which suppresses fork breakage, strand resection, and RPA accumulation. Herein, we use a developed DNA break-detection assay, BrITL, to identify replication-problematic loci that become processed into persistent double-strand breaks across the human genome from ATR inhibition.

2018-10-04 | GSE115623 | GEO

Phosphoproteomics of ATR Signaling in Prophase I of Mouse Meiosis

Project description:Here we used phosphoproteomics to define meiosis-specific ATR signaling events during prophase I in mice following chemical and genetic ablation of ATR signaling. Quantitative analysis of phosphoproteomes obtained after tissue-specific genetic ablation of the ATR activating 9-1-1 complex or treatment with ATR inhibitor revealed over 49,800 phosphorylation sites from testes samples, of which 401 phosphorylation sites were found to be dependent on both the 9-1-1 complex and ATR kinase.

2021-01-25 | MSV000086764 | MassIVE

Transcription profiling of shoot apices from Arabidopsis wild type, teb, atr, and teb atr mutant plants

Project description:Global gene expression patterns were compared among wild-type Col-0, teb, atr, teb atr of A. thaliana using shoot apices.

2008-04-01 | E-MEXP-1329 | biostudies-arrayexpress

Substrates of the ATR kinase - Phosphoproteomics

Project description:Identification and validation of substrates of the ATR kinase by quantitative phosphoproteomics

2024-01-15 | PXD041250 | Pride

RNA processing proteins regulate Mec1/ATR activation by promoting generation of RPA-coated ssDNA.

Project description:Eukaryotic cells respond to DNA double-strand breaks (DSBs) by activating a checkpoint that depends on the protein kinases Tel1/ATM and Mec1/ATR. Mec1/ATR is activated by RPA-coated single-stranded DNA (ssDNA), which arises upon nucleolytic degradation (resection) of the DSB. Emerging evidences indicate that RNA processing factors play critical, yet poorly understood, roles in genomic stability. Here, we provide evidence that the Saccharomyces cerevisiae RNA decay factors Xrn1, Rrp6 and Trf4 regulate Mec1/ATR activation by promoting generation of RPA-coated ssDNA. The lack of Xrn1 inhibits ssDNA generation at the DSB by preventing the loading of the MRX complex. By contrast, DSB resection is not affected in the absence of Rrp6 or Trf4, but their lack impairs the recruitment of RPA, and therefore of Mec1, to the DSB. Rrp6 and Trf4 inactivation affects neither Rad51/Rad52 association nor DSB repair by HR, suggesting that full Mec1 activation requires higher amount of RPA-coated ssDNA than HR-mediated repair. Noteworthy, deep transcriptome analyses do not identify common misregulated gene expression that could explain the observed phenotypes. Our results provide a novel link between RNA processing and genome stability. Strand-specific transcriptome analysis of biological replicates of WT cells (JKM139 strain) at T0, or 60 and 240 minutes after HO induction, and of xrn1∆, rrp6∆ and trf4∆ cells at T0.

2014-11-20 | E-GEOD-63444 | biostudies-arrayexpress

ATR licenses PINK1-mediated mitophagy

Project description:Mitochondria are the central metabolic hub of the cell and their function is vital for cellular activities. Mitochondrial autophagy, or mitophagy, is a quality control mechanism to surveille the fitness and functionality of mitochondria and is therefore essential for life. Both mitochondrial dysfunction and malfunctional DNA damage response (DDR) are a major etiology for tissue impairment and aging. ATR has been shown mainly as a nuclear factor to conduct DNA damage response under DNA replication stress. Paradoxically, the human Seckel syndrome caused by ATR mutations is characterized by premature aging and neuropathies, suggesting a role of ATR in non-replicating tissues. Here we report a previously unknown yet direct role of ATR at mitochondria. We find that HSP90 chaperones ATR and PINK1 to mitochondria, where ATR interacts with and thereby stabilizes PINK1 docking at the mitochondrial translocase TOM/TIM complex as well as with the electron transport chain (ETC). ATR mutant cells are refractory to mitophagy initiation, which can be reverted by an ectopic expression of full length, but not ATR-interaction mutant, PINK1. ATR deletion alters mitochondrial dynamics and OXPHOS functions producing aberrantly high reactive oxygen species (ROS) that attack cytosolic macromolecules prior to damaging nuclear DNA. Intriguingly, pharmacological intervention of mitochondrial metabolism to prevent ROS overproduction can mute ATR-mediated nuclear DDR. This study demonstrates that ATR is an integrated component of the mitochondrial membrane to ensure mitochondrial fitness as a primary physiological function, which, together with its essential DDR function, safeguards the cell fate under physiological and genotoxic conditions.

2025-02-26 | GSE244464 | GEO