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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
Kidae Kim1,2, Sung Goo Park1,3, Byung Chul Park1,2, Jeong-Hoon Kim1,3, Sunhong Kim1,4,*
1Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology,
2Department of Proteome Structural biology and 3Department of Functional Genomics and 4Department of Bio-Molecular Science, Korea University of Science and Technology
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), but a feedback mechanism back to PDK1 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 might affect the kinase activity of PDK1 toward downstream substrates. These results suggest a possible negative feedback loop between PDK1 and ULK1.
Abstract, Accepted Manuscript(in press) [Submitted on December 9, 2019, Accepted on December 19, 2019]
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