Document Detail

CBP and histone deacetylase inhibition enhance the transactivation potential of the HOXB7 homeodomain-containing protein.
MedLine Citation:
PMID:  10435624     Owner:  NLM     Status:  MEDLINE    
Homeodomain-containing proteins are transcription factors regulating the coordinated expression of multiple target genes involved in development, differentiation and cellular transformation. In this study, we demonstrated that HOXB7, one member of this family, behaved as a transactivator in breast cancer cells. Deletion of either the HOXB7 N-terminal domain or the C-terminal acidic tail abolished this transcriptional effect, suggesting a combination of distinct functional transactivating domains. HOXB7 physically interacted both in vitro and in vivo with the coactivator CREB-binding protein (CBP). This interaction led to an enhanced transactivating potential and required the N-terminal of HOXB7 as well as two domains located at the C-terminal part of CBP. Moreover, trichostatin A, a deacetylase inhibitor, strongly enhanced the transcriptional properties of HOXB7. Our data therefore indicate that HOX proteins can directly interact with CBP and that acetylation/deacetylation may regulate their transcriptional properties.
A Chariot; C van Lint; M Chapelier; J Gielen; M P Merville; V Bours
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Oncogene     Volume:  18     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  1999 Jul 
Date Detail:
Created Date:  1999-08-17     Completed Date:  1999-08-17     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  4007-14     Citation Subset:  IM    
Laboratory of Medical Chemistry and Medical Oncology, CHU B35, University of Liege Sart-Tilman, Belgium.
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MeSH Terms
Breast Neoplasms
CREB-Binding Protein
Cyclic AMP Response Element-Binding Protein / physiology*
Drug Synergism
Enzyme Inhibitors / pharmacology
Histone Deacetylase Inhibitors*
Histone Deacetylases / genetics,  physiology*
Homeodomain Proteins / genetics,  physiology*
Nuclear Proteins / physiology*
Peptide Fragments / genetics,  physiology
Plasmids / chemical synthesis
Trans-Activators / genetics,  physiology*
Transcriptional Activation / physiology*
Tumor Cells, Cultured
Reg. No./Substance:
0/CREBBP protein, human; 0/Cyclic AMP Response Element-Binding Protein; 0/Enzyme Inhibitors; 0/HOXB7 protein, human; 0/Histone Deacetylase Inhibitors; 0/Homeodomain Proteins; 0/Nuclear Proteins; 0/Peptide Fragments; 0/Trans-Activators; EC Protein; EC Deacetylases

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