| http://purl.uniprot.org/citations/18765672 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18765672 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18765672 | http://www.w3.org/2000/01/rdf-schema#comment | "The c-myb proto-oncogene product (c-Myb) is degraded in response to Wnt-1 signaling via a pathway involving TAK1 (transforming growth factor-beta-activated kinase 1), HIPK2 (homeodomain-interacting protein kinase 2), and NLK (Nemo-like kinase). NLK directly binds to c-Myb, which results in the phosphorylation of c-Myb at multiple sites, and induces its ubiquitination and proteasome-dependent degradation. Here, we report that Fbxw7, the F-box protein of an SCF complex, targets c-Myb for degradation in a Wnt-1- and NLK-dependent manner. Fbxw7alpha directly binds to c-Myb via its C-terminal WD40 domain and induces the ubiquitination of c-Myb in the presence of NLK in vivo and in vitro. The c-Myb phosphorylation site mutant failed to interact with Fbxw7alpha, suggesting that the c-Myb/Fbxw7alpha interaction is enhanced by NLK phosphorylation of c-Myb. Treatment of M1 cells with Fbxw7 small interfering RNA (siRNA) rescued the Wnt-induced c-Myb degradation and also the Wnt-induced inhibition of cell proliferation. NLK bound to Cul1, a component of the SCF complex, while HIPK2 interacted with both Fbxw7alpha and Cul1, suggesting that both kinases enhance the c-Myb/SCF interaction. In contrast to c-Myb, the v-myb gene product (v-Myb) encoded by the avian myeloblastosis virus was resistant to NLK/Fbxw7alpha-induced degradation. Thus, Fbxw7 is an E3 ubiquitin ligase of c-Myb, and the increased c-Myb levels may contribute, at least partly, to transformation induced by mutation of Fbxw7."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m804340200"xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m804340200"xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Ishii S."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Ishii S."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Watanabe N."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Watanabe N."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Nomura T."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Nomura T."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Takagi T."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Takagi T."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Nakayama K.I."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Nakayama K.I."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Kanei-Ishii C."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/author | "Kanei-Ishii C."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/pages | "30540-30548"xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/pages | "30540-30548"xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/title | "Fbxw7 acts as an E3 ubiquitin ligase that targets c-Myb for nemo-like kinase (NLK)-induced degradation."xsd:string |
| http://purl.uniprot.org/citations/18765672 | http://purl.uniprot.org/core/title | "Fbxw7 acts as an E3 ubiquitin ligase that targets c-Myb for nemo-like kinase (NLK)-induced degradation."xsd:string |