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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2005-12-5
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-10064544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-10347202,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-10366853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-10375510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-10433919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-10766745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-10978285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-11001584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-11022042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-11137451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-11262234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-11290296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-11738817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-11796223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-12042312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-12044012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-12052894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-12101226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-12385751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-12435627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-12888527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-14500813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-15060175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-15242340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-2832761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-2850480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-7673192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-8557628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-9109493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-9699856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16326862-9724649
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6805-15
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16326862-Alcohol Oxidoreductases,
pubmed-meshheading:16326862-Animals,
pubmed-meshheading:16326862-Cell Line,
pubmed-meshheading:16326862-Cell Nucleus,
pubmed-meshheading:16326862-DNA-Binding Proteins,
pubmed-meshheading:16326862-Gene Silencing,
pubmed-meshheading:16326862-Guinea Pigs,
pubmed-meshheading:16326862-Histone Deacetylases,
pubmed-meshheading:16326862-Kruppel-Like Transcription Factors,
pubmed-meshheading:16326862-Mice,
pubmed-meshheading:16326862-Phosphoproteins,
pubmed-meshheading:16326862-Repressor Proteins,
pubmed-meshheading:16326862-Sequence Deletion,
pubmed-meshheading:16326862-Transcriptional Activation,
pubmed-meshheading:16326862-Two-Hybrid System Techniques
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pubmed:year |
2005
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pubmed:articleTitle |
Krüppel-like zinc finger protein Gli-similar 2 (Glis2) represses transcription through interaction with C-terminal binding protein 1 (CtBP1).
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pubmed:affiliation |
Cell Biology Section, Division of Intramural Research, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Intramural
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