May 2006
Volume 47, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2006
Protein Phosphatase–1 Dephosphorylates Pax 6, A Major Transcription Factor In The Ocular Lens
Q. Yan; J.–P. Liu; J. Qin; H. Feng; Y.–M. Xiao; W.–B. Liu; X.–Q. Huang; H.–G. Chen; Y. Liu; D.W. Li
Author Affiliations & Notes
  • Q. Yan
    The Hormel Institute, University of Minnesota, Austin, MN
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • J.–P. Liu
    The Hormel Institute, University of Minnesota, Austin, MN
  • J. Qin
    The Hormel Institute, University of Minnesota, Austin, MN
  • H. Feng
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • Y.–M. Xiao
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • W.–B. Liu
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • X.–Q. Huang
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • H.–G. Chen
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • Y. Liu
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • D.W. Li
    The Hormel Institute, University of Minnesota, Austin, MN
    College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China
  • Footnotes
    Commercial Relationships  Q. Yan, None; J. Liu, None; J. Qin, None; H. Feng, None; Y. Xiao, None; W. Liu, None; X. Huang, None; H. Chen, None; Y. Liu, None; D.W. Li, None.
  • Footnotes
    Support  NIH Grant EY15765
Investigative Ophthalmology & Visual Science May 2006, Vol.47, 2565. doi:
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      Q. Yan, J.–P. Liu, J. Qin, H. Feng, Y.–M. Xiao, W.–B. Liu, X.–Q. Huang, H.–G. Chen, Y. Liu, D.W. Li; Protein Phosphatase–1 Dephosphorylates Pax 6, A Major Transcription Factor In The Ocular Lens . Invest. Ophthalmol. Vis. Sci. 2006;47(13):2565.

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Abstract

Purpose: : Pax 6 is an evolutionarily conserved transcription factor and plays a critical role for the normal development of the eyes in human, mouse, zebrafish, and Drosophila. Previous studies have shown that Pax 6 is a phospho–protein and its phosphorylation by ERK and p38 greatly enhances its transactivation. Here, we present evidence to show that the protein phosphatase–1 dephosphorylates Pax–6 to modulate its function.

Methods: : GST–Pax 6 fusion protein was generated and phosphorylated in vitro by p38 kinase. The phosphorylated Pax 6 was subjected to dephosphorylation by PP–1. Co–immunoprecipitation was used to determine the formation of Pax–6 and PP–1 complex.

Results: : Inhibition of PP–1 with protein phosphatase inhibitor enhances hyperphosphorylation of Pax 6. PP–1 can dephosphorylate Pax 6 in vitro. Pax 6 and PP–1 can form in vivo complex.

Conclusions: : PP–1 may dephosphorylate Pax 6 to modulate its function in lens epithelial cells. Supported by EY 15765, Hormel Foundation, and the Lotus Scholar Professorship Funds from Hunan Province Government and Hunan Normal University.

Keywords: phosphorylation • gene/expression • signal transduction 
© 2006, 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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