通过SGK1对其Ser566残基的磷酸化作用调控Fe65在细胞核中的定位。

Regulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue.

作者信息

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

机构信息

School of Science Education, Chungbuk National University, Cheongju, Korea.

出版信息

BMB Rep. 2008 Jan 31;41(1):41-7. doi: 10.5483/bmbrep.2008.41.1.041.

DOI:10.5483/bmbrep.2008.41.1.041

PMID:18304449

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.

摘要

Fe65通过其PID2元件以及APP蛋白家族的其他成员被表征为衔接蛋白前体（APP）。根据血清和糖皮质激素诱导激酶1（SGK1）的底物特异性信息，我们发现SGK1在Fe65中假定的磷酸化位点存在于其（560）CRVRFLSFLA（569）（X60469）的Ser（566）残基上。因此，我们证明了Fe65和荧光素标记的Fe65肽FITC-（560）CRVRFLSFLA（569）在体外被SGK1磷酸化。使用Ser566磷酸化特异性抗体也证明了Ser（566）残基的磷酸化。磷酸化的Fe65主要存在于细胞核中，而Fe65 S556A突变体主要定位于细胞质中。因此，这些数据表明SGK1使Fe65的Ser（566）残基磷酸化，并且这种磷酸化促进Fe65向细胞核的迁移。