Proteomics

Dataset Information

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ROS-activated ATM-dependent phospho-signaling

ABSTRACT: ATM (ataxia-telangiectasia mutated) protein plays a central role in phosphorylating a network of proteins in response to DNA double strand breaks. These phosphorylated proteins function in signalling pathways designed to maintain the stability of the genome and minimize the risk of disease by controlling cell cycle checkpoints, initiating DNA repair and regulating gene expression. We employed a modified TiSH global quantitative phosphoproteomics approach to identify cytoplasmic proteins altered in their phosphorylation state in control and A-T cells in response to oxidative damage. We demonstrated that ATM was activated by oxidative damage in the cytoplasm as well as in the nucleus and identified a total of 9,612 phosphorylation sites including 6,650 high confidence sites mapping to 2,536 unique proteins.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

DISEASE(S): Ataxia Telangiectasia

SUBMITTER: Mark Graham  

LAB HEAD: Mark Graham

PROVIDER: PXD002850 | Pride | 2016-01-04

REPOSITORIES: Pride

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Publications

Reactive Oxygen Species (ROS)-Activated ATM-Dependent Phosphorylation of Cytoplasmic Substrates Identified by Large-Scale Phosphoproteomics Screen.

Kozlov Sergei V SV   Waardenberg Ashley J AJ   Engholm-Keller Kasper K   Arthur Jonathan W JW   Graham Mark E ME   Lavin Martin M  

Molecular & cellular proteomics : MCP 20151223 3

Ataxia-telangiectasia, mutated (ATM) protein plays a central role in phosphorylating a network of proteins in response to DNA damage. These proteins function in signaling pathways designed to maintain the stability of the genome and minimize the risk of disease by controlling cell cycle checkpoints, initiating DNA repair, and regulating gene expression. ATM kinase can be activated by a variety of stimuli, including oxidative stress. Here, we confirmed activation of cytoplasmic ATM by autophospho  ...[more]

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