An asymmetrically dimethylarginated nuclear 90 kDa protein (p90aDMA) induced by interleukin (IL)-2, IL-4 or IL-6 in the tumor microenvironment is selectively degraded by autophagy.

@article{Sun2016AnAD,
  title={An asymmetrically dimethylarginated nuclear 90 kDa protein (p90aDMA) induced by interleukin (IL)-2, IL-4 or IL-6 in the tumor microenvironment is selectively degraded by autophagy.},
  author={Lei Sun and Wu-Yan Xia and Shao-hua Zhao and Ning Liu and Shan-Shan Liu and Peng Bo Xiu and Lin-Feng Li and Xue-lei Cao and Jian-xin Gao},
  journal={International journal of oncology},
  year={2016},
  volume={48 6},
  pages={
          2461-71
        }
}
Protein arginine methylation is a common posttranslational modification resulting in the generation of asymmetric dimethylarginine (aDMA) and symmetric dimethylarginine (sDMA). Currently, the regulation of aDMA or sDMA by hypoxia, nutrient stavation or cytokines in the tumor microenvironment remains largely unknown. Here we show that p90aDMA, p70aDMA and p90sDMA, endogenous proteins containing aDMA or sDMA with mass 70 or 90 kDa, were widely and dominantly expressed in breast cancer cell lines… CONTINUE READING

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SHOWING 1-10 OF 64 REFERENCES

Arginine methylation of HSP70 regulates retinoid acid-mediated RARβ2 gene activation.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2015
VIEW 1 EXCERPT