A novel corepressor, BCoR-L1, represses transcription through an interaction with CtBP

Pagan, Julia K., Arnold, Jeremy, Hanchard, Kim J., Kumar, Raman, Bruno, Tiziana, Jones, Mathew J.K., Richard, Derek J., Forrest, Alistair, Spurdle, Amanda, Verdin, Eric, Crossley, Merlin, Fanciulli, Maurizio, Chenevix-Trench, Georgia, Young, David B. and Khanna, Kum Kum (2007) A novel corepressor, BCoR-L1, represses transcription through an interaction with CtBP. Journal of Biological Chemistry, 282 20: 15248-15257. doi:10.1074/jbc.M700246200

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Author Pagan, Julia K.
Arnold, Jeremy
Hanchard, Kim J.
Kumar, Raman
Bruno, Tiziana
Jones, Mathew J.K.
Richard, Derek J.
Forrest, Alistair
Spurdle, Amanda
Verdin, Eric
Crossley, Merlin
Fanciulli, Maurizio
Chenevix-Trench, Georgia
Young, David B.
Khanna, Kum Kum
Title A novel corepressor, BCoR-L1, represses transcription through an interaction with CtBP
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2007-05
Sub-type Article (original research)
DOI 10.1074/jbc.M700246200
Open Access Status File (Publisher version)
Volume 282
Issue 20
Start page 15248
End page 15257
Total pages 10
Place of publication Bethesda
Publisher American Society Biochemistry Molecular Biology Inc
Collection year 2008
Language eng
Subject 06 Biological Sciences
0601 Biochemistry and Cell Biology
Abstract Corepressors play a crucial role in negative gene regulation and are defective in several diseases. BCoR is a corepressor for the BCL6 repressor protein. Here we describe and functionally characterize BCoR-L1, a homolog of BCoR. When tethered to a heterologous promoter, BCoR-L1 is capable of strong repression. Like other corepressors, BCoR-L1 associates with histone deacetylase ( HDAC) activity. Specifically, BCoR-L1 coprecipitates with the Class II HDACs, HDAC4, HDAC5, and HDAC7, suggesting that they are involved in its role as a transcriptional repressor. BCoR-L1 also interacts with the CtBP corepressor through a CtBP-interacting motif in its amino terminus. Abrogation of the CtBP binding site within BCoR-L1 partially relieves BCoR-L1-mediated transcriptional repression. Furthermore, BCoR-L1 is located on the E-cadherin promoter, a known CtBP-regulated promoter, and represses the E-cadherin promoter activity in a reporter assay. The inhibition of BCoR-L1 expression by RNA-mediated interference results in derepression of E-cadherin in cells that do not normally express E-cadherin, indicating that BCoR-L1 contributes to the repression of an authentic endogenous CtBP target.
Keyword Biochemistry & Molecular Biology
Ii Histone Deacetylases
Terminal-binding-protein
Epithelial-mesenchymal Transitions
E-cadherin Expression
Co-repressor
Ankyrin-repeat
Genetic-diseases
In-vivo
Acetylation
Identification
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Medicine Publications
 
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Created: Mon, 18 Feb 2008, 17:13:52 EST