Replication stress induced site-specific phosphorylation targets WRN to the ubiquitin-proteasome pathway.

@article{Su2016ReplicationSI,
  title={Replication stress induced site-specific phosphorylation targets WRN to the ubiquitin-proteasome pathway.},
  author={Fengtao Su and Souparno Bhattacharya and Salim Abdisalaam and Shibani Mukherjee and Hirohiko Yajima and Y Claire Yang and Ritu Rathore Shubham Mishra and Kalayarasan Srinivasan and Subroto Ghose and David L. Chen and Steven M. Yannone and Aroumougame Asaithamby},
  journal={Oncotarget},
  year={2016},
  volume={7 1},
  pages={
          46-65
        }
}
Faithful and complete genome replication in human cells is essential for preventing the accumulation of cancer-promoting mutations. WRN, the protein defective in Werner syndrome, plays critical roles in preventing replication stress, chromosome instability, and tumorigenesis. Herein, we report that ATR-mediated WRN phosphorylation is needed for DNA replication and repair upon replication stress. A serine residue, S1141, in WRN is phosphorylated in vivo by the ATR kinase in response to… CONTINUE READING

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Werner Syndrome Protein and DNA Replication

  • International journal of molecular sciences
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