Article
Regulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue.
BMB reports - 31 Jan 2008
Lee Eun Jeoung, Chun Jaesun, Hyun Sunghee, Ahn Hye Rim, Jeong Jae Myung, Hong Soon-Kwang, Hong Jin Tae, Chang In Kyeong, Jeon Hye Yeon, Han Yeon Soo, Auh Chung-Kyoon, Park Jae In, Kang Sang Sun
Abstract excerpt
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...
Topics
- Active Transport, Cell Nucleus
- Amino Acid Substitution
- Animals
- Binding Sites
- COS Cells
- Cell Nucleus
- Cells, Cultured
- Chlorocebus aethiops
- Fluorescent Antibody Technique
- Humans
- Immediate-Early Proteins
- Mutation
- Nerve Tissue Proteins