BMB reports, 2008-01, Vol.41 (1), p.41-47
- Lee, E.J. (Chungbuk National University, Cheongju, Republic of Korea)
- Chun, J.S. (Korea National University of Education, Cheongwon, Republic of Korea)
- Hyun, S.H. (Eulji University School of Medicine, Daejeon, Republic of Korea)
- Ahn, H.R. (Chungbuk National University, Cheongju, Republic of Korea)
- Jeong, J.M. (Korea National University of Education, Cheongwon, Republic of Korea)
- Hong, S.K. (Myongji University, Yongin, Republic of Korea)
- Hong, J.T. (Chungbuk National University, Cheongju, Republic of Korea)
- Chang, I.K. (Chungbuk National University, Cheongju, Republic of Korea)
- Jeon, H.Y. (Chungbuk National University, Cheongju, Republic of Korea)
- Han, Y.S. (Chonnam National University, Gwangju, Republic of Korea)
- Auh, C.K. (Mokpo National University, Muan, Republic of Korea)
- Park, J.I. (Chungbuk National University, Cheongju, Republic of Korea)
- Kang, S.S. (Chungbuk National University, Cheongju, Republic of Korea), E-mail: jin95324@cbu.ac.kr
2008
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- Autor(en) / Beteiligte
- Lee, E.J. (Chungbuk National University, Cheongju, Republic of Korea)
- Chun, J.S. (Korea National University of Education, Cheongwon, Republic of Korea)
- Hyun, S.H. (Eulji University School of Medicine, Daejeon, Republic of Korea)
- Ahn, H.R. (Chungbuk National University, Cheongju, Republic of Korea)
- Jeong, J.M. (Korea National University of Education, Cheongwon, Republic of Korea)
- Hong, S.K. (Myongji University, Yongin, Republic of Korea)
- Hong, J.T. (Chungbuk National University, Cheongju, Republic of Korea)
- Chang, I.K. (Chungbuk National University, Cheongju, Republic of Korea)
- Jeon, H.Y. (Chungbuk National University, Cheongju, Republic of Korea)
- Han, Y.S. (Chonnam National University, Gwangju, Republic of Korea)
- Auh, C.K. (Mokpo National University, Muan, Republic of Korea)
- Park, J.I. (Chungbuk National University, Cheongju, Republic of Korea)
- Kang, S.S. (Chungbuk National University, Cheongju, Republic of Korea), E-mail: jin95324@cbu.ac.kr
- Titel
- Regulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue
- Ist Teil von
- BMB reports, 2008-01, Vol.41 (1), p.41-47
- Ort / Verlag
- Korea (South)
- Erscheinungsjahr
- 2008
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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 ∨560CRVRFLSFLA∨569 (X60469). Thus, we demonstrated that Fe65 and the fluorescein-labeled Fe65 peptide FITC-∨560CRVRFLSFLA∨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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1976-6696DOI: 10.5483/BMBRep.2008.41.1.041Titel-ID: cdi_proquest_miscellaneous_70340830
- Format
- –
- Schlagworte
- Active Transport, Cell Nucleus - physiology, Amino Acid Substitution, Animals, Binding Sites - physiology, Cell Nucleus - metabolism, Cells, Cultured, Cercopithecus aethiops, Confocal microscopy, COS Cells, fe65, Fluorescent Antibody Technique, Humans, Immediate-Early Proteins - metabolism, localization, Mutation, Nerve Tissue Proteins - genetics, Nerve Tissue Proteins - metabolism, Nuclear Proteins - genetics, Nuclear Proteins - metabolism, Phosphorylation, protein phosphorylation, protein-protein interaction, Protein-Serine-Threonine Kinases - metabolism, PROTEINAS, PROTEINE, PROTEINS, Rats, Recombinant Proteins - genetics, Recombinant Proteins - metabolism, SGK1, subcellular