April 2009
Volume 50, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2009
Protein Serine/Threonine Phosphatase-1 Regulates PI3K-AKT Pathway
D. Yuan; L. Xiao; L. Zhang; J. Liu; M. Deng; L. Gong; X.-F. Hu; W.-B. Liu; Y.-M. Xiao; D. W. Li
Author Affiliations & Notes
  • D. Yuan
    Key Lab of Protein Chemistry & Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • L. Xiao
    Key Lab of Protein Chemistry & Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • L. Zhang
    Key Lab of Protein Chemistry & Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • J. Liu
    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
  • X.-F. Hu
    Key Lab of Protein Chemistry & Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • W.-B. Liu
    Key Lab of Protein Chemistry & Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • Y.-M. Xiao
    Key Lab of Protein Chemistry & Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • D. W. Li
    Key Lab of Protein Chemistry & Developmental Biology of Education Ministry of China, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
    Biochemistry & Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska
  • Footnotes
    Commercial Relationships  D. Yuan, None; L. Xiao, None; L. Zhang, None; J. Liu, None; M. Deng, None; L. Gong, None; X.-F. Hu, None; W.-B. Liu, None; Y.-M. Xiao, None; D.W. Li, None.
  • Footnotes
    Support  1R01EY015765, UNMC start-up funds, Lotus Scholar Prefessorship Funds, Changjiang Scholar Team Award, Key Lab Funds
Investigative Ophthalmology & Visual Science April 2009, Vol.50, 4352. doi:
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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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Abstract

Purpose: : 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.

Methods: : 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.

Results: : 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.

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

Keywords: cell survival • cataract • signal transduction 
© 2009, The Association for Research in Vision and Ophthalmology, Inc., all rights reserved. Permission to republish any abstract or part of an abstract in any form must be obtained in writing from the ARVO Office prior to publication.
Copyright © 2025 Association for Research in Vision and Ophthalmology.
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