Document Detail


Dephosphorylation of Rb (Thr-821) in response to cell stress.
MedLine Citation:
PMID:  16764854     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The retinoblastoma tumor suppressor Rb is regulated by reversible phosphorylation that is dependent upon cyclin-dependent kinase (CDK) and protein phosphatase type 1 (PP1) activity in replicating cells. Hyperphosphorylated Rb allows cells to proliferate, whereas the hypophosphorylated isoform of Rb inhibits proliferation. Of the many phosphorylation sites of Rb, there is functional information available for a very few. In this report, we show that threonine-821 (Thr-821) of Rb is dephosphorylated earlier than other phosphorylation sites when cells are grown under hypoxic conditions which leads to Rb activation and G(1) arrest. This finding is interesting because Thr-821 of Rb remains phosphorylated throughout the cell division cycle in replicating cells. We hypothesized that the phosphorylation state of Thr-821 of Rb may depend on cellular stress. We report in this study that, when nontransformed CV1 epithelial cells and Hs578T breast cancer cells are treated with the chemotherapeutic agent cytosine arabinoside (Ara-C), Thr-821 of Rb is rapidly dephosphorylated concomitant with dissociation of the PP1 regulatory subunit PNUTS (phosphatase nuclear targeting subunit) from PP1 enzyme. These data are consistent with the concept that differential regulation of Rb-directed phosphatase activity exists when cells are progressing through the cell cycle compared to that observed when cells are under stress.
Authors:
Nancy A Krucher; Ethel Rubin; Vivienne C Tedesco; Michael H Roberts; Tara C Sherry; Gabriel De Leon
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2006-05-10
Journal Detail:
Title:  Experimental cell research     Volume:  312     ISSN:  0014-4827     ISO Abbreviation:  Exp. Cell Res.     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-08-25     Completed Date:  2006-10-19     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0373226     Medline TA:  Exp Cell Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2757-63     Citation Subset:  IM    
Affiliation:
Department of Biology and Health Sciences, Pace University, 109 Dyson Hall, 861 Bedford Road, Pleasantville, NY 10570, USA. nkrucher@pace.edu
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MeSH Terms
Descriptor/Qualifier:
Antimetabolites, Antineoplastic / metabolism,  pharmacology
Cell Cycle / drug effects
Cell Hypoxia
Cytarabine / metabolism,  pharmacology
DNA-Binding Proteins / metabolism
Epithelial Cells / cytology,  metabolism
Female
Humans
Nuclear Proteins / metabolism
Phosphoprotein Phosphatases / metabolism
Phosphorylation / drug effects
Protein Subunits / metabolism
RNA-Binding Proteins / metabolism
Retinoblastoma Protein / metabolism*
Threonine / metabolism
Tumor Cells, Cultured
Grant Support
ID/Acronym/Agency:
R15 CA 88803-01A2/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Antimetabolites, Antineoplastic; 0/DNA-Binding Proteins; 0/Nuclear Proteins; 0/PPP1R10 protein, human; 0/Protein Subunits; 0/RNA-Binding Proteins; 0/Retinoblastoma Protein; 147-94-4/Cytarabine; 72-19-5/Threonine; EC 3.1.3.16/Phosphoprotein Phosphatases

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


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