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http://purl.uniprot.org/citations/11483589http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11483589http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11483589http://www.w3.org/2000/01/rdf-schema#comment"The DF3/MUC1 mucin-like, transmembrane glycoprotein is aberrantly overexpressed in most human carcinomas. The MUC1 cytoplasmic domain interacts with the c-Src tyrosine kinase and thereby increases binding of MUC1 and beta-catenin. In the present work, coimmunoprecipitation studies demonstrate that MUC1 associates constitutively with the epidermal growth factor receptor (EGF-R) in human ZR-75-1 breast carcinoma cells. Immunofluorescence studies show that EGF-R and MUC1 associate at the cell membrane. We also show that the activated EGF-R phosphorylates the MUC1 cytoplasmic tail on tyrosine at a YEKV motif that functions as a binding site for the c-Src SH2 domain. The results demonstrate that EGF-R-mediated phosphorylation of MUC1 induces binding of MUC1 to c-Src in cells. Moreover, in vitro and in vivo studies demonstrate that EGF-R increases binding of MUC1 and beta-catenin. These findings support a novel role for EGF-R in regulating interactions of MUC1 with c-Src and beta-catenin."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100359200"xsd:string
http://purl.uniprot.org/citations/11483589http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100359200"xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Kuwahara H."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Kuwahara H."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Li Q."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Li Q."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Kufe D."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Kufe D."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Ren J."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Ren J."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Yu W."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Yu W."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Yin L."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Yin L."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Carraway K.L. III"xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/author"Carraway K.L. III"xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11483589http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string