May 2004
Volume 45, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2004
Dephosphorylation of the Tumor Suppressor, p53, at the N–terminal Serine/Threonine Sites Modulates Its Transactivity and Apoptotic Ability
H. Feng; X.–Q. Huang; Y. Liu; J.–P. Liu; S.–J. Liu; C. Luo; Y. Liu; D.W. Li
Author Affiliations & Notes
  • H. Feng
    Coll Life Sci, Hunan Normal Univ, Changsha, China
  • X.–Q. Huang
    Coll Life Sci, Hunan Normal Univ, Changsha, China
  • Y. Liu
    Coll Life Sci, Hunan Normal Univ, Changsha, China
  • J.–P. Liu
    The Hormel Institute, University of Minnesota, Austin, MN
  • S.–J. Liu
    Coll Life Sci, Hunan Normal Univ, Changsha, China
  • C. Luo
    Coll Life Sci, Hunan Normal Univ, Changsha, China
  • Y. Liu
    Coll Life Sci, Hunan Normal Univ, Changsha, China
  • D.W. Li
    Coll Life Sci, Hunan Normal Univ, Changsha, China
    The Hormel Institute, University of Minnesota, Austin, MN
  • Footnotes
    Commercial Relationships  H. Feng, None; X. Huang, None; Y. Liu, None; J. Liu, None; S. Liu, None; C. Luo, None; Y. Liu, None; D.W. Li, None.
  • Footnotes
    Support  none
Investigative Ophthalmology & Visual Science May 2004, Vol.45, 402. doi:
  • Views
  • Share
  • Tools
    • Alerts
      User Alerts
      You are adding an alert for:
      Dephosphorylation of the Tumor Suppressor, p53, at the N–terminal Serine/Threonine Sites Modulates Its Transactivity and Apoptotic Ability
      You will receive an email whenever this article is corrected, updated, or cited in the literature. You can manage this and all other alerts in My Account
      The alert will be sent to:
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation
      Citation

      H. Feng, X.–Q. Huang, Y. Liu, J.–P. Liu, S.–J. Liu, C. Luo, Y. Liu, D.W. Li; Dephosphorylation of the Tumor Suppressor, p53, at the N–terminal Serine/Threonine Sites Modulates Its Transactivity and Apoptotic Ability . Invest. Ophthalmol. Vis. Sci. 2004;45(13):402.

      Download citation file:

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

      ×
    • Get Permissions
  • Supplements
Abstract

Abstract: : Purpose: Our previous studies have demonstrated that protein phosphatase–1 (PP–1) is important in promoting survival of lens epithelial cells. Recent studies have revealed that PP–1 may exert its antiapoptotic function through dephosphorylation of p53. In the present study, we have compared the function of wild type and mutated p53 in mediating transactivation and apoptosis in lens and non–lens cells. Methods: PCR–linked in vitro mutagenesis was used to generate the following mutations: S15A and S20A. The function of these mutants in regulating apoptosis and also expression of the downstream apoptosis–related genes were compared with wild type p53 in human lens epithelial cells with p53 knocked out and p53 –/– tumor cell line, DU145. Results: Mutation of the phosphorylation sites at Ser–15 and Ser–20 modulates both the transactivity and apoptotic ability of p53. Conclusions: Dephosphorylation of p53 plays an role in its function mediating apoptosis. Supported by the Hormel Foundation, University of Minnesota Graduate School and Lotus Scholar Professorship funds from Hunan Normal University. None.

Keywords: phosphorylation • signal transduction • cell death/apoptosis 
© 2004, 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.
×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×
This site uses cookies. By continuing to use our website, you are agreeing to our privacy policy.Accept