Source:http://linkedlifedata.com/resource/pubmed/id/15710417
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2005-2-15
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pubmed:abstractText |
The DNA-binding protein recombination signal-binding protein-Jk (RBP-J) plays a key role in transcriptional regulation by targeting the intracellular domain of Notch (NIC) and the Epstein-Barr virus nuclear antigen 2 (EBNA2) to specific promoters. In the absence of the Notch signaling, RBP-J acts as a transcriptional suppressor through recruiting co-suppressors such as histone deacetylase (HDAC). KyoT2 is a LIM domain protein that suppresses the RBP-J-mediated transcriptional activation. In the current study, we show that the polycomb group (PcG) protein HPC2, which functions as a transcriptional suppressor, is a candidate of KyoT2-binding proteins. To confirm the physical and functional interaction between KyoT2 and HPC2, we carried out yeast two-hybrid, GST-pull down, co-immunoprecipitation, as well as mammalian two-hybrid assays. Our results showed HPC2 and KyoT2 interacted both in vitro and in vivo, probably through the C-terminal fragment of HPC2 and LIM domains of KyoT2. In addition, we also found that overexpression of HPC2, not only inhibited transactivation of a RBP-J-dependent promoter by NIC, but also transactivation by RBP-J-VP16, a constitutively active form of RBP-J. Taken together, our results suggested that KyoT2 might inhibit the RBP-J-mediated transactivation through NIC by recruiting co-suppressors such as HPC2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin J Recombination...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RBPJ protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/polycomb group proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
579
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1220-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15710417-Cell Line,
pubmed-meshheading:15710417-DNA-Binding Proteins,
pubmed-meshheading:15710417-Humans,
pubmed-meshheading:15710417-Immunoglobulin J Recombination Signal Sequence-Binding...,
pubmed-meshheading:15710417-Immunoprecipitation,
pubmed-meshheading:15710417-Membrane Proteins,
pubmed-meshheading:15710417-Multiprotein Complexes,
pubmed-meshheading:15710417-Muscle Proteins,
pubmed-meshheading:15710417-Nuclear Proteins,
pubmed-meshheading:15710417-Promoter Regions, Genetic,
pubmed-meshheading:15710417-Protein Binding,
pubmed-meshheading:15710417-Receptors, Notch,
pubmed-meshheading:15710417-Repressor Proteins,
pubmed-meshheading:15710417-Transcription, Genetic,
pubmed-meshheading:15710417-Transcriptional Activation
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pubmed:year |
2005
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pubmed:articleTitle |
The PcG protein HPC2 inhibits RBP-J-mediated transcription by interacting with LIM protein KyoT2.
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pubmed:affiliation |
State Key Laboratory of GI Cancer Biology, Department of Medical Genetics and Developmental Biology, Fourth Military Medical University, Chang-Le Xi Street, Xi'an 710032, Shaanxi Province, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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