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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Regulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue

  • Lee, Eun-Jeoung (School of Science Education, Chungbuk National University) ;
  • Chun, Jae-Sun (Department of Biological Education, Korea National University of Education) ;
  • Hyun, Sung-Hee ;
  • Ahn, Hye-Rim (School of Science Education, Chungbuk National University) ;
  • Jeong, Jae-Myung (Department of Biological Education, Korea National University of Education) ;
  • Hong, Soon-Kwang (Division of Life Science, Myungji University) ;
  • Hong, Jin-Tae (Department of Pharmacy, Chungbuk National University) ;
  • Chang, In-Kyeong (School of Science Education, Chungbuk National University) ;
  • Jeon, Hye-Yeon (School of Science Education, Chungbuk National University) ;
  • Han, Yeon-Soo (Department of Agricultural Biology, Chonnam National University) ;
  • Auh, Chung-Kyoon (Division of Applied Biotechnology, Mokpo National University) ;
  • Park, Jae-In (Department of Forest Science, Chungbuk National University) ;
  • Kang, Sang-Sun (School of Science Education, Chungbuk National University)
  • Published : 2008.01.31
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Abstract

Fe65 is characterized as an adaptor precursor (APP) through its PID2 element, as well as with the other members of the APP protein family. With the serum- and glucocorticoid-induced kinase 1 (SGK1) substrate specificity information, we found that the putative site of phosphorylation in Fe65 by SGK1 is present on its $Ser^{566}$ residue in $^{560}CRVRFLSFLA^{569}$(X60469). Thus, we demonstrated that Fe65 and the fluorescein-labeled Fe65 peptide $FITC-^{560}CRVRFLSFLA^{569}$ are phosphorylated in vitro by SGK1. Phosphorylation of the $Ser^{566}$ residue was also demonstrated using a $Ser^{566}$ phospho-specific antibody. The phospho Fe65 was found mainly in the nucleus, while Fe65 S556A mutant was localized primarily to the cytoplasm. Therefore, these data suggest that SGK1 phosphorylates the $Ser^{566}$ residue of Fe65 and that this phosphorylation promotes the migration of Fe65 to the nucleus of the cell.

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References

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