Document Detail


Phosphorylation of the retinoblastoma-related protein p130 in growth-arrested cells.
MedLine Citation:
PMID:  11042701     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The retinoblastoma family of proteins including pRB, p107 and p130 undergoes cell cycle dependent phosphorylation during the mid-G1 to S phase transition. This phosphorylation is dependent upon the activity of cyclin D/cdk4. In contrast to pRB and p107, p130 is phosphorylated during G0 and the early G1 phase of the cell cycle. We observed that p130 is specifically phosphorylated on serine and threonine residues in T98G cells arrested in G0 by serum deprivation or density arrest. Identification of the phospho-serine and phospho-threonine residues revealed that most were clustered within a short co-linear region unique to p130, defined as the Loop. Deletion of the Loop region resulted in a change in the phosphorylation status of p130 under growth arrest conditions. Notably, deletion of the Loop did not affect the ability of p130 to bind to E2F-4 or SV40 Large T antigen, to induce growth arrest in Saos-2 cells, and to become hyperphosphorylated during the proliferative phase of the cell cycle. p130 undergoes specific G0 phosphorylation in a manner that distinguishes it from pRB and p107.
Authors:
A J Canhoto; A Chestukhin; L Litovchick; J A DeCaprio
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Oncogene     Volume:  19     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  2000 Oct 
Date Detail:
Created Date:  2000-10-26     Completed Date:  2000-10-30     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  5116-22     Citation Subset:  IM    
Affiliation:
Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts, MA 02115, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Antigens, Polyomavirus Transforming / metabolism
Cell Division / physiology
Culture Media, Serum-Free
DNA-Binding Proteins / metabolism
E2F4 Transcription Factor
G0 Phase / physiology*
Glioblastoma / metabolism,  pathology
Mice
Molecular Sequence Data
Phosphoproteins / metabolism*
Phosphorylation
Protein Structure, Tertiary
Proteins*
Rats
Retinoblastoma-Like Protein p130
Transcription Factors / metabolism
Transfection
Tumor Cells, Cultured
Grant Support
ID/Acronym/Agency:
2T32CA09361/CA/NCI NIH HHS; 5T32CA09031/CA/NCI NIH HHS; R01-CA63113/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, Polyomavirus Transforming; 0/Culture Media, Serum-Free; 0/DNA-Binding Proteins; 0/E2F4 Transcription Factor; 0/Phosphoproteins; 0/Proteins; 0/Rbl2 protein, mouse; 0/Rbl2 protein, rat; 0/Retinoblastoma-Like Protein p130; 0/Transcription Factors

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


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