Dimitrova Nadya, de Lange Titia
Laboratory for Cell Biology and Genetics, The Rockefeller University, 1230 York Avenue, New York, NY 10065-6399, USA.
Mol Cell Biol. 2009 Oct;29(20):5552-63. doi: 10.1128/MCB.00476-09. Epub 2009 Aug 10.
Here, we address the role of the MRN (Mre11/Rad50/Nbs1) complex in the response to telomeres rendered dysfunctional by deletion of the shelterin component TRF2. Using conditional NBS1/TRF2 double-knockout MEFs, we show that MRN is required for ATM signaling in response to telomere dysfunction. This establishes that MRN is the only sensor for the ATM kinase and suggests that TRF2 might block ATM signaling by interfering with MRN binding to the telomere terminus, possibly by sequestering the telomere end in the t-loop structure. We also examined the role of the MRN/ATM pathway in nonhomologous end joining (NHEJ) of damaged telomeres. NBS1 deficiency abrogated the telomere fusions that occur in G(1), consistent with the requirement for ATM and its target 53BP1 in this setting. Interestingly, NBS1 and ATM, but not H2AX, repressed NHEJ at dysfunctional telomeres in G(2), specifically at telomeres generated by leading-strand DNA synthesis. Leading-strand telomere ends were not prone to fuse in the absence of either TRF2 or MRN/ATM, indicating redundancy in their protection. We propose that MRN represses NHEJ by promoting the generation of a 3' overhang after completion of leading-strand DNA synthesis. TRF2 may ensure overhang formation by recruiting MRN (and other nucleases) to newly generated telomere ends. The activation of the MRN/ATM pathway by the dysfunctional telomeres is proposed to induce resection that protects the leading-strand ends from NHEJ when TRF2 is absent. Thus, the role of MRN at dysfunctional telomeres is multifaceted, involving both repression of NHEJ in G(2) through end resection and induction of NHEJ in G(1) through ATM-dependent signaling.
在这里,我们探讨了MRN(Mre11/Rad50/Nbs1)复合体在对因缺失端粒保护蛋白组分TRF2而功能失调的端粒的应答中的作用。利用条件性NBS1/TRF2双敲除的小鼠胚胎成纤维细胞(MEFs),我们发现MRN是对端粒功能失调进行ATM信号传导所必需的。这表明MRN是ATM激酶的唯一传感器,并提示TRF2可能通过干扰MRN与端粒末端的结合来阻断ATM信号传导,可能是通过将端粒末端隔离在t环结构中。我们还研究了MRN/ATM途径在受损端粒的非同源末端连接(NHEJ)中的作用。NBS1缺陷消除了G1期发生的端粒融合,这与该情况下ATM及其靶点53BP1的需求一致。有趣的是,NBS1和ATM,而不是H2AX,在G2期抑制功能失调端粒处的NHEJ,特别是在由前导链DNA合成产生的端粒处。在前导链DNA合成完成后,在没有TRF2或MRN/ATM的情况下,前导链端粒末端不易融合,表明它们在保护方面存在冗余。我们提出,MRN通过在前导链DNA合成完成后促进3'突出端的产生来抑制NHEJ。TRF2可能通过将MRN(和其他核酸酶)招募到新产生的端粒末端来确保突出端的形成。功能失调的端粒激活MRN/ATM途径被认为会诱导切除,从而在没有TRF2时保护前导链末端免受NHEJ的影响。因此,MRN在功能失调端粒处的作用是多方面的,包括通过末端切除在G2期抑制NHEJ以及通过ATM依赖的信号传导在G1期诱导NHEJ。