ATG16L1 phosphorylation is oppositely regulated by CSNK2/casein kinase 2 and PPP1/protein phosphatase 1 which determines the fate of cardiomyocytes during hypoxia/reoxygenation

@article{Song2015ATG16L1PI,
  title={ATG16L1 phosphorylation is oppositely regulated by CSNK2/casein kinase 2 and PPP1/protein phosphatase 1 which determines the fate of cardiomyocytes during hypoxia/reoxygenation},
  author={Hui-wen Song and J. Pu and L. Wang and Lihua Wu and Jian-Min Xiao and Qigong Liu and J. Chen and Min Zhang and Yang Liu and Mingke Ni and Jinggang Mo and Yunliang Zheng and Deli Wan and X. Cai and Yaping Cao and Weiyi Xiao and L. Ye and Enyuan Tu and Zhi-Huan Lin and Jianxin Wen and X. Lu and J. He and Yi Peng and Jingcai Su and Heng Zhang and Y. Zhao and Meihua Lin and Zhiyong Zhang},
  journal={Autophagy},
  year={2015},
  volume={11},
  pages={1308 - 1325}
}
Recent studies have shown that the phosphorylation and dephosphorylation of ULK1 and ATG13 are related to autophagy activity. Although ATG16L1 is absolutely required for autophagy induction by affecting the formation of autophagosomes, the post-translational modification of ATG16L1 remains elusive. Here, we explored the regulatory mechanism and role of ATG16L1 phosphorylation for autophagy induction in cardiomyocytes. We showed that ATG16L1 was a phosphoprotein, because phosphorylation of… Expand
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  • Medicine, Biology
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  • 2020
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