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http://purl.uniprot.org/citations/9334332http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9334332http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9334332http://www.w3.org/2000/01/rdf-schema#comment"DCC (deleted in colorectal cancer) is postulated to function as transmembrane receptor for the axon and cell guidance factor netrin-1. We report here that the DCC cytoplasmic domain binds to proteins encoded by mammalian homologs of the Drosophila seven in absentia (sina) gene, as well as Drosophila Sina. Sina has a critical role in R7 photoreceptor development and shows upward of 85% amino acid identity with its mammalian homologs (termed Siahs), but the function of the Sina/Siah proteins has not been defined. We sought, therefore, to characterize further their interaction with DCC. Immunofluorescence studies suggested the Sina/Siah proteins localized predominantly in the cytoplasm and in association with DCC. DCC was found to be ubiquitinated and the Sina/Siah proteins regulated its expression. Proteasome inhibitors blocked the effects of Sina/Siah on DCC, and the Sina/Siah proteins interacted with ubiquitin-conjugating enzymes (Ubcs). A mutant Siah protein lacking the amino-terminal Ubc-binding sequences complexed with DCC, but did not degrade it. The in vivo interaction between Sina/Siah and DCC was confirmed through studies of transgenic Drosophila lines in which DCC and Sina were ectopically expressed in the eye. Taken together, the data imply that the Sina/Siah proteins regulate DCC and perhaps other proteins via the ubiquitin-proteasome pathway."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.org/dc/terms/identifier"doi:10.1101/gad.11.20.2701"xsd:string
http://purl.uniprot.org/citations/9334332http://purl.org/dc/terms/identifier"doi:10.1101/gad.11.20.2701"xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Hu G."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Hu G."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Xu T."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Xu T."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Vidal M."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Vidal M."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Fearon E.R."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Fearon E.R."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Baer J.L."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/author"Baer J.L."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/pages"2701-2714"xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/pages"2701-2714"xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/title"Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway."xsd:string
http://purl.uniprot.org/citations/9334332http://purl.uniprot.org/core/title"Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway."xsd:string