Document Detail

A new function for p53 ubiquitination.
MedLine Citation:
PMID:  17110328     Owner:  NLM     Status:  MEDLINE    
The amount of p53 protein in a cell is normally limited by ubiquitin-dependent degradation. In this issue of Cell, Le Cam et al. (2006) reveal that p53 ubiquitination contributes to transcriptional activation rather than protein stability. These results may provide insight into how p53 can modulate diverse cellular processes such as growth arrest and apoptosis.
Yuko Hirano; Ze'ev Ronai
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Publication Detail:
Type:  Comment; Journal Article    
Journal Detail:
Title:  Cell     Volume:  127     ISSN:  0092-8674     ISO Abbreviation:  Cell     Publication Date:  2006 Nov 
Date Detail:
Created Date:  2006-11-19     Completed Date:  2006-12-22     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0413066     Medline TA:  Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  675-7     Citation Subset:  IM    
Burnham Institute for Medical Research, La Jolla, CA 92130, USA.
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MeSH Terms
Cell Cycle Proteins / metabolism
Histone Acetyltransferases / metabolism
Lysine / metabolism
Proto-Oncogene Proteins c-mdm2 / metabolism
Repressor Proteins / chemistry,  metabolism
Transcription Factors / metabolism
Tumor Suppressor Protein p53 / metabolism*
Ubiquitin-Protein Ligases / metabolism*
p300-CBP Transcription Factors
Reg. No./Substance:
0/Cell Cycle Proteins; 0/E4F1 protein, human; 0/Repressor Proteins; 0/Transcription Factors; 0/Tumor Suppressor Protein p53; 56-87-1/Lysine; EC Acetyltransferases; EC Transcription Factors; EC factor; EC protein, human; EC Proteins c-mdm2; EC Ligases
Comment On:
Cell. 2006 Nov 17;127(4):775-88   [PMID:  17110336 ]

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

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