Source:http://linkedlifedata.com/resource/pubmed/id/16583136
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2006-8-31
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pubmed:abstractText |
The nuclear matrix protein Msx2-interacting nuclear target protein (MINT) is a transcription factor that regulates the expression of key transcriptional effectors in diverse signaling pathways. To further understand the function and mechanism of the MINT-mediated transcription regulation, the yeast two-hybrid system was employed to screen proteins that interact with the C-terminal fragment of MINT. From a cDNA library of human lymph nodes, a cDNA encoding the ubiquitin-conjugating enzyme UbcH8 was identified. Using different truncated versions of MINT, we show that the C-terminal Spen paralog and ortholog C-terminal domain (SPOC) domain, which has been demonstrated to mediate interactions between MINT and a panel of other molecules, might be responsible for interaction between MINT and UbcH8 in yeast, as confirmed by the beta-galactosidase assay. The interaction between MINT and UbcH8 in mammalian cells was further proved by a series of biochemical assays including the mammalian two-hybrid assay, GST pull-down assay, and co-immunoprecipitation assay. Using a reporter system, we found that MINT-mediated transcription suppression was sensitive to MG132, an inhibitor of the proteosome system. These results suggest a novel mechanism of MINT-mediated transcription regulation, and might be helpful for understanding functions of MINT.
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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/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Leupeptins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SPEN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/UBE2L6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/benzyloxycarbonylleucyl-leucyl-leuci...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0300-8177
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
288
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
151-7
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pubmed:meshHeading |
pubmed-meshheading:16583136-Animals,
pubmed-meshheading:16583136-Binding Sites,
pubmed-meshheading:16583136-COS Cells,
pubmed-meshheading:16583136-Cells, Cultured,
pubmed-meshheading:16583136-Cercopithecus aethiops,
pubmed-meshheading:16583136-HeLa Cells,
pubmed-meshheading:16583136-Homeodomain Proteins,
pubmed-meshheading:16583136-Humans,
pubmed-meshheading:16583136-Leupeptins,
pubmed-meshheading:16583136-Nuclear Proteins,
pubmed-meshheading:16583136-Signal Transduction,
pubmed-meshheading:16583136-Transcription, Genetic,
pubmed-meshheading:16583136-Two-Hybrid System Techniques,
pubmed-meshheading:16583136-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:16583136-Ubiquitins
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pubmed:year |
2006
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pubmed:articleTitle |
The Spen homolog Msx2-interacting nuclear target protein interacts with the E2 ubiquitin-conjugating enzyme UbcH8.
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pubmed:affiliation |
State Key Laboratory of Cancer Biology, Department of Medical Genetics and Developmental Biology, Fourth Military Medical University, Changle Xi Street #17, Xian, 710032, P. R. China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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