pubmed-article:17336575 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17336575 | lifeskim:mentions | umls-concept:C0206588 | lld:lifeskim |
pubmed-article:17336575 | lifeskim:mentions | umls-concept:C0084913 | lld:lifeskim |
pubmed-article:17336575 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:17336575 | lifeskim:mentions | umls-concept:C0596260 | lld:lifeskim |
pubmed-article:17336575 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:17336575 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:17336575 | pubmed:dateCreated | 2007-4-20 | lld:pubmed |
pubmed-article:17336575 | pubmed:abstractText | Small ubiquitin-related modifier (SUMO) is a protein moiety that is ligated to lysine residues in a variety of target proteins. The SUMO E2 enzyme ubiquitin-conjugating enzyme 9 (Ubc9) is sufficient for substrate recognition and lysine modification of known SUMO targets. Previous studies have demonstrated that mutated Ubc9 that has lost its SUMO-ligating activity retains its enhancement on transactivation mediated by androgen receptor (AR). In contrast to the binding ability to Ubc9, the sumoylation of AR via the association of SUMO-1 and PIAS1 is able to repress AR-dependent transcription. In the present study, we present several lines of evidence to explain the role of over-expressed Ubc9 as a cofactor in the nuclear receptor and coactivator functions, including (i) activity that is independent of its ability to catalyze SUMO-1 conjugation, (ii) an insight into the protein-protein interaction motif in its eight C-terminal residues, (iii) selective coactivator function in nuclear receptor-relevant transactivation activities, and (iv) a non-trichostatin A-sensitive autonomous transcription repression domain in its far C-terminal region. Taken together, our data suggest that the both the protein-protein interaction through the Ubc9 C-terminus and its sumoylation-modifying activity provide the mechanism for regulating nuclear receptor functions. | lld:pubmed |
pubmed-article:17336575 | pubmed:language | eng | lld:pubmed |
pubmed-article:17336575 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17336575 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17336575 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17336575 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17336575 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17336575 | pubmed:issn | 1357-2725 | lld:pubmed |
pubmed-article:17336575 | pubmed:author | pubmed-author:HuangShih-Min... | lld:pubmed |
pubmed-article:17336575 | pubmed:author | pubmed-author:HuangChi-Jung... | lld:pubmed |
pubmed-article:17336575 | pubmed:author | pubmed-author:LiuPei-YaoPY | lld:pubmed |
pubmed-article:17336575 | pubmed:author | pubmed-author:ChanJames... | lld:pubmed |
pubmed-article:17336575 | pubmed:author | pubmed-author:ChangHui-Ping... | lld:pubmed |
pubmed-article:17336575 | pubmed:author | pubmed-author:ChangYung-Lun... | lld:pubmed |
pubmed-article:17336575 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17336575 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:17336575 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17336575 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17336575 | pubmed:pagination | 1035-46 | lld:pubmed |
pubmed-article:17336575 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:17336575 | pubmed:meshHeading | pubmed-meshheading:17336575... | lld:pubmed |
pubmed-article:17336575 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17336575 | pubmed:articleTitle | Regulation of nuclear receptor and coactivator functions by the carboxyl terminus of ubiquitin-conjugating enzyme 9. | lld:pubmed |
pubmed-article:17336575 | pubmed:affiliation | Department of Biochemistry, National Defense Medical Center, Taipei 114, Taiwan, ROC. | lld:pubmed |
pubmed-article:17336575 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17336575 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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