Purchase this article with an account.
D. Yuan, J. Liu, Q. Yan, H.-G. Chen, M. Deng, L. Gong, D. W. Li; Protein Phosphatase-1 Dephosphorylates Akt1 at Ser-450 to Regulate Its Activation. Invest. Ophthalmol. Vis. Sci. 2008;49(13):1901. doi: https://doi.org/.
Download citation file:
© ARVO (1962-2015); The Authors (2016-present)
The PI3K-Akt pathway plays an very important role in promoting survival of the lens epithelial cells. Although its activation by different kinases have been elucidated, its inactivation is not fully understood. In the present study, we have discovered that the protein serine/threonine phosphatase-1 is involved in regulating Akt1 activation through its action on the Ser-450 residue.
In vitro and in vivo dephosphorylation assays, co-immunoprecipitation and RNAi were used to demonstrate that PP-1 dephosphorylates Akt1 at Ser-450. In vitro mutagenesis was used to generate constant phosphorylate and dephosphorylated Akt1 mutants at Ser-450.
PP-1 and Akt1 can form complex. Inhibition of PP-1 or knockdown of PP-1 by RNAi greatly enhances Akt1 hyperphosdphorylation at Ser-450. In vitro and in vivo dephosphorylation assays suggest that PP-1 dephosphorylates Akt-1.
PP-1 dephosphorylates Akt1 at Ser-450 to modulate Akt1 activation and this modulation may be involved in regulation of lens differentiation.
This PDF is available to Subscribers Only