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http://purl.uniprot.org/citations/16904669http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16904669http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16904669http://www.w3.org/2000/01/rdf-schema#comment"TRIM11 is a member of the tripartite-motif-containing protein family and is known to destabilize humanin, an inhibitor of Alzheimer-like neuronal insults. In this study, we demonstrate that TRIM11 interacts with activator-recruited cofactor 105-kDa component (ARC105) that mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling. Co-expression of TRIM11 increased ARC105 degradation but a proteasome inhibitor suppressed this. Co-expression of TRIM11 and ARC105 also increased ubiquitination of ARC105. In addition, TRIM11 suppressed ARC105-mediated transcriptional activation induced with TGFbeta in a reporter assay. These results suggest that TRIM11, with the ubiquitin-proteasome pathway, regulates ARC105 function in TGFbeta signaling."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2006.07.066"xsd:string
http://purl.uniprot.org/citations/16904669http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2006.07.066"xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Ishikawa H."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Ishikawa H."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Takahashi N."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Takahashi N."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Tachikawa H."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Tachikawa H."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Miura Y."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/author"Miura Y."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/pages"4784-4792"xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/pages"4784-4792"xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/title"TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/title"TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system."xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/volume"580"xsd:string
http://purl.uniprot.org/citations/16904669http://purl.uniprot.org/core/volume"580"xsd:string
http://purl.uniprot.org/citations/16904669http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16904669
http://purl.uniprot.org/citations/16904669http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16904669