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Journal ArticleDOI

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage

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TLDR
A large-scale proteomic analysis of proteins phosphorylated in response to DNA damage on consensus sites recognized by ATM and ATR is performed and more than 900 regulated phosphorylation sites encompassing over 700 proteins are identified.
Abstract
Cellular responses to DNA damage are mediated by a number of protein kinases, including ATM (ataxia telangiectasia mutated) and ATR (ATM and Rad3-related). The outlines of the signal transduction portion of this pathway are known, but little is known about the physiological scope of the DNA damage response (DDR). We performed a large-scale proteomic analysis of proteins phosphorylated in response to DNA damage on consensus sites recognized by ATM and ATR and identified more than 900 regulated phosphorylation sites encompassing over 700 proteins. Functional analysis of a subset of this data set indicated that this list is highly enriched for proteins involved in the DDR. This set of proteins is highly interconnected, and we identified a large number of protein modules and networks not previously linked to the DDR. This database paints a much broader landscape for the DDR than was previously appreciated and opens new avenues of investigation into the responses to DNA damage in mammals.

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Journal ArticleDOI

Radiation-induced double-strand breaks require ATM but not Artemis for homologous recombination during S-phase

TL;DR: It is shown that during S-phase Artemis but not ATM is dispensable for HR of radiation-induced DSBs, and it is demonstrated that in AT cells loading of Rad51 depends on functional ATR/Chk1.
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Beyond the Trinity of ATM, ATR, and DNA-PK: Multiple Kinases Shape the DNA Damage Response in Concert With RNA Metabolism.

TL;DR: Kinase-dependent phosphorylation events on RNAPII, Drosha and Dicer, and 53BP1 that modulate the key steps of the DDR to DSBs and UVR are reviewed, suggesting an intimate link between the DDR and RNA metabolism.
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Reading chromatin signatures after DNA double-strand breaks

TL;DR: How the modified chromatin surrounding DSBs is read is reviewed, with a focus on the insights gleaned from structural and biochemical studies.
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PIKK-dependent phosphorylation of Mre11 induces MRN complex inactivation by disassembly from chromatin

TL;DR: This study provides a functional characterization of the DNA damage-induced Mre11 phosphorylation, and suggests that MRN inactivation participates in the down-regulation of damage signaling during checkpoint recovery following DSB repair.
Journal ArticleDOI

BRCT domains: A little more than kin, and less than kind.

TL;DR: The biology of BRCT domains is discussed and how a domain‐centric analysis can aid in the understanding of signal transduction events in the DNA damage response network.
References
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Journal ArticleDOI

The DNA damage response: putting checkpoints in perspective

TL;DR: The inability to repair DNA damage properly in mammals leads to various disorders and enhanced rates of tumour development, and this work has shown that direct activation of DNA repair networks is needed to correct this problem.
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Cell-cycle checkpoints and cancer

TL;DR: All life on earth must cope with constant exposure to DNA-damaging agents such as the Sun's radiation, and how cells respond to DNA damage are critical determinants of whether that individual will develop cancer.
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DNA damage-induced activation of p53 by the checkpoint kinase Chk2.

TL;DR: Chk2 directly phosphorylated p53 on serine 20, which is known to interfere with Mdm2 binding, and provides a mechanism for increased stability of p53 by prevention of ubiquitination in response to DNA damage.
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Immunoaffinity profiling of tyrosine phosphorylation in cancer cells

TL;DR: Applying this approach to several cell systems, including cancer cell lines, shows it can be used to identify activated protein kinases and their phosphorylated substrates without prior knowledge of the signaling networks that are activated, a first step in profiling normal and oncogenic signaling networks.
Journal Article

Global Analysis of Protein Phosphorylation in Yeast

TL;DR: The in vitro substrates recognized by most yeast protein kinases are described, with the use of proteome chip technology, and these results will provide insights into the mechanisms and roles of protein phosphorylation in many eukaryotes.
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