title: Regulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue.
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 Ser566 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.
authors.affiliation: School of Science Education, Chungbuk National University, Cheongju, Korea.
authors.forename: Eun Jeoung
authors.initials: EJ
authors.lastname: Lee
authors.forename: Jaesun
authors.initials: J
authors.lastname: Chun
authors.forename: Sunghee
authors.initials: S
authors.lastname: Hyun
authors.forename: Hye Rim
authors.initials: HR
authors.lastname: Ahn
authors.forename: Jae Myung
authors.initials: JM
authors.lastname: Jeong
authors.forename: Soon-Kwang
authors.initials: SK
authors.lastname: Hong
authors.forename: Jin Tae
authors.initials: JT
authors.lastname: Hong
authors.forename: In Kyeong
authors.initials: IK
authors.lastname: Chang
authors.forename: Hye Yeon
authors.initials: HY
authors.lastname: Jeon
authors.forename: Yeon Soo
authors.initials: YS
authors.lastname: Han
authors.forename: Chung-Kyoon
authors.initials: CK
authors.lastname: Auh
authors.forename: Jae In
authors.initials: JI
authors.lastname: Park
authors.forename: Sang Sun
authors.initials: SS
authors.lastname: Kang
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000502:physiology; D019943:Amino Acid Substitution; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D019556:COS Cells; D002467:Cell Nucleus / Q000378:metabolism*; D002478:Cells, Cultured; D002522:Chlorocebus aethiops; D005455:Fluorescent Antibody Technique; D006801:Humans; D017874:Immediate-Early Proteins / Q000378:metabolism*; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism*; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D000099184:Serum-Glucocorticoid Regulated Kinases
chemical_list: D017874:Immediate-Early Proteins; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D017346:Protein Serine-Threonine Kinases; D011994:Recombinant Proteins; D000099184:Serum-Glucocorticoid Regulated Kinases; C486242:Apbb1 protein, rat