微球体蛋白 2 与 ASK1 结合，并作为应激诱导的 ASK1 激活的负调节剂发挥作用。
Microspherule protein 2 associates with ASK1 and acts as a negative regulator of stress-induced ASK1 activation.
机构信息
State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, PR China.
出版信息
FEBS Lett. 2012 Jun 12;586(12):1678-86. doi: 10.1016/j.febslet.2012.04.051. Epub 2012 May 15.
Microspherule protein 2 (MCRS2) has been reported to associate with the cellular function of telomerase inhibition, transcriptional regulation and cellular transformation. Here, we report a novel function of MCRS2 in ASK1 pathway. We found that MCRS2 directly binds to ASK1 in vivo and co-localises with ASK1 in the cytoplasm. Overexpression of MCRS2 inhibited oxidative stress (H(2)O(2))-induced ASK1 activation. Knockdown of MCRS2 expression accelerated p38 and JNK phosphorylation and promoted apoptosis in response to H(2)O(2). Finally, H(2)O(2) treatment induced proteasomal degradation of MCRS2, which was further enhanced by activated ASK1. Our results clearly demonstrate that MCRS2 plays a negative role in stress-induced ASK1 activation.
微球体蛋白 2（MCRS2）已被报道与端粒酶抑制、转录调控和细胞转化的细胞功能有关。在这里，我们报告了 MCRS2 在 ASK1 途径中的一个新功能。我们发现 MCRS2 可在体内直接与 ASK1 结合，并在细胞质中与 ASK1 共定位。MCRS2 的过表达抑制了氧化应激（H2O2）诱导的 ASK1 激活。MCRS2 表达的下调加速了 p38 和 JNK 的磷酸化，并促进了对 H2O2 的凋亡。最后，H2O2 处理诱导了 MCRS2 的蛋白酶体降解，而激活的 ASK1 进一步增强了这一过程。我们的结果清楚地表明，MCRS2 在应激诱导的 ASK1 激活中起负性作用。
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