Document Detail

Interaction of PP2A catalytic subunit with Rb2/p130 is required for all-trans retinoic acid suppression of ovarian carcinoma cell growth.
MedLine Citation:
PMID:  16206244     Owner:  NLM     Status:  MEDLINE    
All-trans retinoic acid (ATRA) treatment causes CAOV3 ovarian carcinoma cells to growth arrest in the G0/G1 phase and to elevate the level of Rb2/p130 protein. PP2A, a serine/threonine phosphatase, binds and dephosphorylates Rb2/p130, thereby increasing the half-life of Rb2/p130 in the cell. In order to further characterize the interaction between Rb2/p130 and PP2A upon ATRA treatment, we examined the posttranslational modification of PP2A. ATRA treatment leads to hypophosphorylation of PP2A catalytic subunit (PP2Ac) that correlates with increased PP2A activity. In addition, the N-terminus of PP2Ac binds directly to NLS sequences located in the C-terminus of Rb2/p130. Furthermore, CAOV3 cells transfected with a truncated Rb2/p130 construct consisting of only the wt C-terminus grew more aggressively and were less sensitive to ATRA treatment when compared to parental CAOV3 cells. In contrast, CAOV3 cells transfected with a truncated Rb2/p130 construct consisting of only the C-terminus in which the NLS sites were mutated and which could not interact with PP2A, were as sensitive to ATRA treatment as parental CAOV3 cells. These studies suggest that ATRA treatment suppresses the growth of CAOV3 cells via a novel posttranscriptional mechanism involving PP2A.
Enkhtsetseg Purev; Antonio Giordano; Dianne Robert Soprano; Kenneth J Soprano
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Journal of cellular physiology     Volume:  206     ISSN:  0021-9541     ISO Abbreviation:  J. Cell. Physiol.     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2005-12-05     Completed Date:  2006-03-10     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0050222     Medline TA:  J Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  495-502     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2005 Wiley-Liss, Inc.
Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
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MeSH Terms
Catalytic Domain
Cell Line, Tumor
Cell Proliferation / drug effects
Ovarian Neoplasms / metabolism*,  pathology
Phosphoprotein Phosphatases / chemistry,  metabolism*
Protein Processing, Post-Translational
Retinoblastoma-Like Protein p130 / chemistry,  genetics,  pharmacology*,  physiology*
Tretinoin / pharmacology*
Grant Support
Reg. No./Substance:
0/Retinoblastoma-Like Protein p130; 302-79-4/Tretinoin; EC Phosphatases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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