Iwahori Satoko, Kohmon Daisuke, Kobayashi Junya, Tani Yuhei, Yugawa Takashi, Komatsu Kenshi, Kiyono Tohru, Sugimoto Nozomi, Fujita Masatoshi
Virology Division; National Cancer Center Research Institute; Chuohku, Tokyo, Japan.
Department of Cellular Biochemistry; Graduate School of Pharmaceutical Sciences; Kyushu University; Higashiku, Fukuoka, Japan.
Cell Cycle. 2014;13(3):471-81. doi: 10.4161/cc.27274. Epub 2013 Nov 26.
Ataxia-telangiectasia mutated (ATM) plays crucial roles in DNA damage responses, especially with regard to DNA double-strand breaks (DSBs). However, it appears that ATM can be activated not only by DSB, but also by some changes in chromatin architecture, suggesting potential ATM function in cell cycle control. Here, we found that ATM is involved in timely degradation of Cdt1, a critical replication licensing factor, during the unperturbed S phase. At least in certain cell types, degradation of p27(Kip1) was also impaired by ATM inhibition. The novel ATM function for Cdt1 regulation was dependent on its kinase activity and NBS1. Indeed, we found that ATM is moderately phosphorylated at Ser1981 during the S phase. ATM silencing induced partial reduction in levels of Skp2, a component of SCF(Skp2) ubiquitin ligase that controls Cdt1 degradation. Furthermore, Skp2 silencing resulted in Cdt1 stabilization like ATM inhibition. In addition, as reported previously, ATM silencing partially prevented Akt phosphorylation at Ser473, indicative of its activation, and Akt inhibition led to modest stabilization of Cdt1. Therefore, the ATM-Akt-SCF(Skp2) pathway may partly contribute to the novel ATM function. Finally, ATM inhibition rendered cells hypersensitive to induction of re-replication, indicating importance for maintenance of genome stability.
共济失调毛细血管扩张症突变基因(ATM)在DNA损伤反应中起着关键作用,特别是在DNA双链断裂(DSB)方面。然而,似乎ATM不仅可以被DSB激活,还可以被染色质结构的一些变化激活,这表明ATM在细胞周期控制中具有潜在功能。在这里,我们发现ATM在正常的S期参与关键复制许可因子Cdt1的及时降解。至少在某些细胞类型中,ATM抑制也会损害p27(Kip1)的降解。ATM对Cdt1调控的新功能依赖于其激酶活性和NBS1。事实上,我们发现ATM在S期Ser1981位点发生适度磷酸化。ATM沉默导致SCF(Skp2)泛素连接酶控制Cdt1降解的组分Skp2水平部分降低。此外,Skp2沉默导致Cdt1稳定,类似于ATM抑制。另外,如先前报道,ATM沉默部分阻止了Akt在Ser473位点的磷酸化,这表明其被激活,并且Akt抑制导致Cdt1适度稳定。因此,ATM-Akt-SCF(Skp2)途径可能部分促成了ATM的新功能。最后,ATM抑制使细胞对再复制诱导高度敏感,表明其对维持基因组稳定性的重要性。