Skip Navigation

Nucleic Acids Research 2005 33(21):6805-6815; doi:10.1093/nar/gki985
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (549K) Freely available
Right arrow Screen PDF (556K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (8)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kim, S.-C.
Right arrow Articles by Jetten, A. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kim, S.-C.
Right arrow Articles by Jetten, A. M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 2 December 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Krüppel-like zinc finger protein Gli-similar 2 (Glis2) represses transcription through interaction with C-terminal binding protein 1 (CtBP1)

Seong-Chul Kim, Yong-Sik Kim and Anton M. Jetten*

Cell Biology Section, Division of Intramural Research, National Institute of Environmental Health Sciences, National Institutes of Health Research Triangle Park, NC 27709, USA

*To whom correspondence should be addressed. Tel: +1 919 541 2768; Fax: +1 919 541 4133; Email: jetten{at}niehs.nih.gov

Received November 9, 2005. Accepted November 10, 2005.

Glis2 is a member of the Gli-similar (Glis) subfamily of Krüppel-like zinc finger transcription factors. It functions as an activator and repressor of gene transcription. To identify potential co-activators or co-repressors that mediate these actions of Glis2, we performed yeast two-hybrid analysis using Glis2 as bait. C-terminal binding protein 1 (CtBP1) was identified as one of the proteins that interact with Glis2. This interaction was confirmed by mammalian two-hybrid analysis. CtBP1 did not interact with other members of the Glis subfamily suggesting that this interaction is specific for Glis2. Pulldown analysis with GST-CtBP1 demonstrated that CtBP1 physically interacts with Glis2. Analysis of CtBP1 and Glis2 deletion mutants identified several regions important for this interaction. CtBP1 repressed transcriptional activation induced by Glis2(1–171). Repression by Glis2 appears to involve the recruitment of both CtBP1 and histone deacetylase 3 (HDAC3). Confocal microscopic analysis demonstrated that Glis2 localized to nuclear speckles while in most cells CtBP1 was found diffusely in both cytoplasm and nucleus. However, when CtBP1 and Glis2 were co-expressed, CtBP1 was restricted to nuclear speckles and co-localized with Glis2. Our observations suggest that the co-repressor CtBP1 and HDAC3 are part of transcription silencing complex that mediates the transcriptional repression by Glis2.

Correspondence may also be addressed to Yong-Sik Kim. Tel: +1 919 541 4702; Fax: +1 919 541 4133; Email: kim13{at}niehs.nih.gov


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
H. S. Kang, Y.-S. Kim, G. ZeRuth, J. Y. Beak, K. Gerrish, G. Kilic, B. Sosa-Pineda, J. Jensen, J. Foley, and A. M. Jetten
Transcription Factor Glis3, a Novel Critical Player in the Regulation of Pancreatic {beta}-Cell Development and Insulin Gene Expression
Mol. Cell. Biol., December 15, 2009; 29(24): 6366 - 6379.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
H. S. Kang, J. Y. Beak, Y.-S. Kim, R. Herbert, and A. M. Jetten
Glis3 Is Associated with Primary Cilia and Wwtr1/TAZ and Implicated in Polycystic Kidney Disease
Mol. Cell. Biol., May 15, 2009; 29(10): 2556 - 2569.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
Y.-S. Kim, H. S. Kang, R. Herbert, J. Y. Beak, J. B. Collins, S. F. Grissom, and A. M. Jetten
Kruppel-Like Zinc Finger Protein Glis2 Is Essential for the Maintenance of Normal Renal Functions
Mol. Cell. Biol., April 1, 2008; 28(7): 2358 - 2367.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
J. Y. Beak, H. S. Kang, Y.-S. Kim, and A. M. Jetten
Functional analysis of the zinc finger and activation domains of Glis3 and mutant Glis3(NDH1)
Nucleic Acids Res., March 1, 2008; 36(5): 1690 - 1702.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
C. R. Hosking, F. Ulloa, C. Hogan, E. C. Ferber, A. Figueroa, K. Gevaert, W. Birchmeier, J. Briscoe, and Y. Fujita
The Transcriptional Repressor Glis2 Is a Novel Binding Partner for p120 Catenin
Mol. Biol. Cell, May 1, 2007; 18(5): 1918 - 1927.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
K. G. R. Quinlan, A. Verger, A. Kwok, S. H. Y. Lee, J. Perdomo, M. Nardini, M. Bolognesi, and M. Crossley
Role of the C-Terminal Binding Protein PXDLS Motif Binding Cleft in Protein Interactions and Transcriptional Repression
Mol. Cell. Biol., November 1, 2006; 26(21): 8202 - 8213.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y. Wang, E. O. Gracheva, J. Richmond, T. Kawano, J. M. Couto, J. A. Calarco, V. Vijayaratnam, Y. Jin, and M. Zhen
The C2H2 zinc-finger protein SYD-9 is a putative posttranscriptional regulator for synaptic transmission
PNAS, July 5, 2006; 103(27): 10450 - 10455.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.