Linked Life Data

17336575

Source:http://linkedlifedata.com/resource/pubmed/id/17336575

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-4-20
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1357-2725
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1035-46
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:17336575-Animals, pubmed-meshheading:17336575-Blotting, Western, pubmed-meshheading:17336575-COS Cells, pubmed-meshheading:17336575-Carrier Proteins, pubmed-meshheading:17336575-Cell Line, Tumor, pubmed-meshheading:17336575-Cercopithecus aethiops, pubmed-meshheading:17336575-HeLa Cells, pubmed-meshheading:17336575-Humans, pubmed-meshheading:17336575-Plasmids, pubmed-meshheading:17336575-Protein Binding, pubmed-meshheading:17336575-Receptors, Androgen, pubmed-meshheading:17336575-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:17336575-Small Ubiquitin-Related Modifier Proteins, pubmed-meshheading:17336575-Transcription Factors, pubmed-meshheading:17336575-Transcriptional Activation, pubmed-meshheading:17336575-Transfection, pubmed-meshheading:17336575-Ubiquitin-Conjugating Enzymes
pubmed:year
2007
pubmed:articleTitle
Regulation of nuclear receptor and coactivator functions by the carboxyl terminus of ubiquitin-conjugating enzyme 9.
pubmed:affiliation
Department of Biochemistry, National Defense Medical Center, Taipei 114, Taiwan, ROC.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't