Research ResourcePhosphoproteomics

ATM-Dependent and -Independent Dynamics of the Nuclear Phosphoproteome After DNA Damage

See allHide authors and affiliations

Science Signaling  07 Dec 2010:
Vol. 3, Issue 151, pp. rs3
DOI: 10.1126/scisignal.2001034

You are currently viewing the editor's summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Beyond ATM in the DNA Damage Response

Because genome stability is essential to cellular and organismal survival, cells have evolved elaborate mechanisms to respond to DNA damage. A key protein involved in the initiation of the cellular response to DNA double-strand breaks, which can be caused by chemicals or radiation, is the protein kinase ATM. Bensimon et al. performed a quantitative analysis of the phosphoproteomic changes that occurred in response to double-strand breaks and found that a large proportion of the changes in phosphorylation were not attributable to ATM activity, suggesting a much larger kinase-mediated phosphorylation network in this critical response. Bioinformatic analysis suggested several candidate kinases that carry out the ATM-independent phosphorylations. Mapping sites that showed decreased phosphorylation in response to DNA damage suggested kinases that might be inhibited or whose action might be reversed by phosphatases activated during the DNA damage response. In addition to revealing a previously unknown phosphorylation site on ATM implicated in its retention at sites of damage, this study also provides a plethora of opportunities for deeper investigation into the phosphorylation network involved in maintaining genome stability.

View Full Text

Stay Connected to Science Signaling