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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Serine 389 phosphorylation of 3-phosphoinositide-dependent kinase 1 by UNC-51-like kinase 1 affects its ability to regulate Akt and p70 S6kinase

  • Kim, Kidae (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Park, Sung Goo (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Park, Byoung Chul (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Jeong-Hoon (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Sunhong (Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology)
  • Received : 2019.12.09
  • Accepted : 2019.12.19
  • Published : 2020.07.31
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Abstract

Phosphorylation of the signaling component by protein kinase often leads to a kinase cascade or feedback loop. 3-Phosphoinositide-dependent kinase 1 (PDK1) signaling pathway diverges into various kinases including Akt and p70 S6 kinase (p70S6k). However, the PDK1 feedback mechanism remains elusive. Here, we demonstrated that UNC-51-like kinase (ULK1), an autophagy initiator kinase downstream of mechanistic target of rapamycin (mTOR), directly phosphorylated PDK1 on serine 389 at the linker region. Furthermore, our data showed that this phosphorylation affected the kinase activity of PDK1 toward downstream substrates. These results suggest a possible negative feedback loop between PDK1 and ULK1.

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References

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