May 2008
Volume 49, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2008
Protein Phosphatase-1 Dephosphorylates Akt1 at Ser-450 to Regulate Its Activation
Author Affiliations & Notes
  • D. Yuan
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • J. Liu
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • Q. Yan
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • H.-G. Chen
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • M. Deng
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • L. Gong
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • D. W. Li
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • Footnotes
    Commercial Relationships  D. Yuan, None; J. Liu, None; Q. Yan, None; H. Chen, None; M. Deng, None; L. Gong, None; D.W. Li, None.
  • Footnotes
    Support  NIH/NEI 1R01EY15765, and UNMC.
Investigative Ophthalmology & Visual Science May 2008, Vol.49, 1901. doi:https://doi.org/
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    • Get Citation

      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/.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: : 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.

Methods: : 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.

Results: : 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.

Conclusions: : PP-1 dephosphorylates Akt1 at Ser-450 to modulate Akt1 activation and this modulation may be involved in regulation of lens differentiation.

Keywords: phosphorylation • apoptosis/cell death • cell survival 
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