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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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Recent findings and technological advances in phosphoproteomics for cells and tissues

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Chromatin at the nuclear periphery and the regulation of genome functions

TL;DR: The mechanisms underlying the attachment of chromatin at the nuclear lamina or the nuclear pores are reviewed, their plasticity and their consequences on the regulation of gene expression, DNA repair and replication are reviewed.
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Enigmatic roles of Mcm10 in DNA replication

TL;DR: The essential role in DNA replication initiation is not mutually exclusive with additional functions that Mcm10 may have as part of the elongation machinery, and existing controversies are discussed.
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A Pleiotropic RNA-Binding Protein Controls Distinct Cell Cycle Checkpoints to Drive Resistance of p53-Defective Tumors to Chemotherapy

TL;DR: It is shown that the RNA binding protein hnRNPA0 is the "successor" to p53 for checkpoint control, demonstrating the importance of post-transcriptional RNA control to chemotherapy response.
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.
Journal ArticleDOI

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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