| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871245 | FEBS Letters | 2012 | 6 Pages |
Abstract
⺠NOK overexpression leads to enhanced phosphorylation of GSK-3β at its Ser9 residue. ⺠NOK could make complexes with both Akt and GSK-3β. ⺠NOK could promote Akt phosphorylation at Thr308 but not Ser473. ⺠Knockdown of Akt disrupted NOK-dependent GSK-3β (Ser9) phosphorylation. ⺠NOK, p-Akt (Thr308) and p-GSK-3β (Ser9) were positively correlated in vivo.
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Authors
Jing Li, Fang Wu, Feng Sheng, Yi-Jia Li, Da Jin, Xue Ding, Shuping Zhang,