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http://purl.uniprot.org/citations/23082202http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23082202http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23082202http://www.w3.org/2000/01/rdf-schema#comment"Control of cellular proliferation is critical to cell viability. The F-box protein Fbw7 (hAgo/hCdc4/FBXW7) functions as a specificity factor for the Skp1-Cul1-F-box protein (SCF) ubiquitin ligase complex and targets several proteins required for cellular proliferation for ubiquitin-mediated destruction. Fbw7 exists as three splice variants but the mechanistic role of each is not entirely clear. We examined the regulation of the Fbw7-γ isoform, which has been implicated in the degradation of c-Myc. We show here that Fbw7-γ is an unstable protein and that its turnover is proteasome-dependent in transformed cells. Using a two-hybrid screen, we identified a novel interaction partner, SLP-1, which binds the N-terminal domain of Fbw7-γ. Overexpression of SLP-1 inhibits the degradation of Fbw7-γ, suggesting that this interaction can happen in vivo. When Fbw7-γ is stabilized by overexpression of SLP-1, c-Myc protein abundance decreases, suggesting that the SCF(Fbw7-γ) complex maintains activity. We demonstrate that Cdk2 also binds the N-terminal domain of Fbw7-γ as well as SLP-1. Interestingly, co-expression of Cdk2 and SLP-1 does not inhibit Fbw7-γ degradation, suggesting that Cdk2 and SLP-1 may have opposing functions."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0047736"xsd:string
http://purl.uniprot.org/citations/23082202http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0047736"xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/author"Zhang W."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/author"Zhang W."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/author"Koepp D.M."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/author"Koepp D.M."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/author"MacDonald E.M."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/author"MacDonald E.M."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/pages"E47736"xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/pages"E47736"xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/title"The stomatin-like protein SLP-1 and Cdk2 interact with the F-Box protein Fbw7-gamma."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/title"The stomatin-like protein SLP-1 and Cdk2 interact with the F-Box protein Fbw7-gamma."xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/23082202http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/23082202http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23082202
http://purl.uniprot.org/citations/23082202http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23082202
http://purl.uniprot.org/citations/23082202http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23082202
http://purl.uniprot.org/citations/23082202http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23082202