Burrows Anna E, Elledge Stephen J
Department of Genetics, Center for Genetics and Genomics, Brigham and Women's Hospital, Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Genes Dev. 2008 Jun 1;22(11):1416-21. doi: 10.1101/gad.1685108.
In this issue of Genes & Development, Mordes and colleagues (pp. 1478-1489) reveal intriguing mechanistic insights into activation of the ATR (ATM and Rad3-related) kinase critical for DNA damage resistance. They identify conserved regulatory domains within ATR and its binding partner ATRIP (ATR-interacting protein), which are contacted by the ATR activator TopBP1. These discoveries expand on our understanding of the regulation of other PIKK family members, which also contain these domains, and illustrate how functional diversity has been achieved among these kinases.
在本期《基因与发育》中，莫德斯及其同事（第1478 - 1489页）揭示了关于对DNA损伤抗性至关重要的ATR（ATM和Rad3相关）激酶激活的有趣机制见解。他们确定了ATR及其结合伴侣ATRIP（ATR相互作用蛋白）内的保守调节结构域，ATR激活剂TopBP1会与这些结构域接触。这些发现拓展了我们对其他也包含这些结构域的PIKK家族成员调控的理解，并阐明了这些激酶是如何实现功能多样性的。
