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http://purl.uniprot.org/citations/17387146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17387146http://www.w3.org/2000/01/rdf-schema#comment"Apoptosis is critical for embryonic development, tissue homeostasis, and tumorigenesis and is determined largely by the Bcl-2 family of antiapoptotic and prosurvival regulators. Here, we report that glycogen synthase kinase 3 (GSK-3) was required for Mcl-1 degradation, and we identified a novel mechanism for proteasome-mediated Mcl-1 turnover in which GSK-3beta associates with and phosphorylates Mcl-1 at one consensus motif ((155)STDG(159)SLPS(163)T; phosphorylation sites are in italics), which will lead to the association of Mcl-1 with the E3 ligase beta-TrCP, and beta-TrCP then facilitates the ubiquitination and degradation of phosphorylated Mcl-1. A variant of Mcl-1 (Mcl-1-3A), which abolishes the phosphorylations by GSK-3beta and then cannot be ubiquitinated by beta-TrCP, is much more stable than wild-type Mcl-1 and able to block the proapoptotic function of GSK-3beta and enhance chemoresistance. Our results indicate that the turnover of Mcl-1 by beta-TrCP is an essential mechanism for GSK-3beta-induced apoptosis and contributes to GSK-3beta-mediated tumor suppression and chemosensitization."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00620-06"xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"He X."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Xia W."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Zhong Q."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Li L.Y."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Ding Q."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Hung M.C."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Liu J.C."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Chen C.T."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Hsu J.M."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/author"Lee D.F."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/name"Mol Cell Biol"xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/pages"4006-4017"xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/title"Degradation of Mcl-1 by beta-TrCP mediates glycogen synthase kinase 3-induced tumor suppression and chemosensitization."xsd:string
http://purl.uniprot.org/citations/17387146http://purl.uniprot.org/core/volume"27"xsd:string
http://purl.uniprot.org/citations/17387146http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17387146
http://purl.uniprot.org/citations/17387146http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17387146
http://purl.uniprot.org/uniprot/#_A0A087WT64-mappedCitation-17387146http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17387146
http://purl.uniprot.org/uniprot/#_A0A0S2Z4Q5-mappedCitation-17387146http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17387146
http://purl.uniprot.org/uniprot/#_A0A0S2Z507-mappedCitation-17387146http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17387146
http://purl.uniprot.org/uniprot/#_A0A286YDI3-mappedCitation-17387146http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17387146