Akt phosphorylation is essential for nuclear translocation and retention in NGF-stimulated PC12 cells |
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Authors: | Xuan Nguyen Truong Le Choi Joung Woo Lee Sang Bae Ye Keqiang Woo Soo-Dong Lee Kyung-Hoon Ahn Jee-Yin |
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Institution: | Department of Molecular Cell Biology, Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Republic of Korea. |
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Abstract: | Nerve growth factor (NGF) elicits Akt translocation into the nucleus, where it phosphorylates nuclear targets. Here, we describe that Akt phosphorylation can promote the nuclear translocation of Akt and is necessary for its nuclear retention. Overexpression of Akt-K179A, T308A, S473A-mutant failed to show either nuclear translocation or nuclear Akt phosphorylation, whereas expression of wild-type counterpart elicited profound Akt phosphorylation and induced nuclear translocation under NGF stimulation. Employing the PI3K inhibitor and a variety of mutants PI3K, we showed that nuclear translocation of Akt was mediated by activation of PI3K, and Akt phosphorylation status in the nucleus required PI3K activity. Thus the activity of PI3K might contribute to the nuclear translocation of Akt, and that Akt phosphorylation is essential for its nuclear retention under NGF stimulation conditions. |
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Keywords: | Akt Nerve growth factor (NGF) Phosphoinositide 3-kinase (PI3K) PC12 cells Phosphorylation |
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