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D. Yuan, L. Xiao, L. Zhang, J. Liu, M. Deng, L. Gong, X.-F. Hu, W.-B. Liu, Y.-M. Xiao, D. W. Li; Protein Serine/Threonine Phosphatase-1 Regulates PI3K-AKT Pathway. Invest. Ophthalmol. Vis. Sci. 2009;50(13):4352.
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The PI3K-Akt pathway plays a very important role in promoting survival of ocular tissue cells. Its activation is not fully understood. In the present study, we have demonstrated that the protein serine/threonine phosphatase-1 directly dephosphorylates Akt1 to negatively regulate its activation.
In vitro and in vivo dephosphorylation assays, co-immunoprecipitation and RNAi were used to demonstrate that PP-1 directly dephosphorylates Akt1. In vitro mutagenesis and reporter gene activity assays were used to explore the functional changes before and after Akt1 activation in both lens epithelial cells and retinal pigmental epithelial cells.
PP-1 and Akt1 can form complex. Inhibition of PP-1 or knockdown of PP-1 by RNAi greatly enhances Akt1 hyperphosdphorylation. In vitro and in vivo dephosphorylation assays suggest that PP-1 dephosphorylates Akt-1. Dephosphorylation of Akt-1 by PP-1 promotes Akt1 inactivation.
PP-1 dephosphorylates Akt1 to modulate Akt1 activation and this modulation may be involved in regulation of lens differentiation and retinal degeneration.
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