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http://purl.uniprot.org/citations/12734385http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12734385http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12734385http://www.w3.org/2000/01/rdf-schema#comment"Ligand activation of the epidermal growth factor receptor (EGFR) causes the binding of Cbls, which leads to EGFR polyubiquitination and internalization through endophilin complexes that contain the adaptor protein SH3-domain encoding, expressed in tumorigenic astrocytes/Cbl-interacting protein of 85 kDa/regulator of ubiquitous kinase (SETA/CIN85/Ruk). In cells grown at high density, high levels of SETA interfered in the recruitment of Casitas B-lineage (Cbl) proteins to the EGFR and reduced its polyubiquitination, suggesting that SETA has a regulatory function in the formation of the EGFR-Cbl-endophilin complex and in EGFR down-regulation. In a situation where there is EGFR signaling but no internalization or down-regulation, as is the case with the EGFR with exons 2-7 deleted (DeltaEGFR) oncogene, these proteins were absent altogether. By using mAb 806, which recognizes an EGFR-activation state and preferentially immunoprecipitates DeltaEGFR, we show that DeltaEGFR did not interact with Cbls, SETA, or endophilin A1, providing a mechanistic explanation for its lack of internalization. As would be expected by the absence of Cbl proteins in the DeltaEGFR complex, the mutant receptor was also not polyubiquitinated. The intracellular C terminus and tyrosine autophosphorylation pattern of DeltaEGFR are similar to wild-type EGFR, but it signals at a lower intensity as determined by levels of EGFR phosphotyrosine. To test the implication that the lack of interaction with the Cbl-SETA-endophilin complex is because of differences in signal intensity, EGFR-expressing cells were treated with tyrphostin AG1478 EGFR inhibitor. Attenuation of wild-type EGFR signal to levels similar to that found in DeltaEGFR resulted in the dissociation of SETA and Cbl proteins and a concomitant attenuation of receptor internalization."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1031790100"xsd:string
http://purl.uniprot.org/citations/12734385http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1031790100"xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Bogler O."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Bogler O."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Schmidt M.H."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Schmidt M.H."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Cavenee W.K."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Cavenee W.K."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Furnari F.B."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/author"Furnari F.B."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/pages"6505-6510"xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/pages"6505-6510"xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/title"Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/title"Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization."xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/volume"100"xsd:string
http://purl.uniprot.org/citations/12734385http://purl.uniprot.org/core/volume"100"xsd:string
http://purl.uniprot.org/citations/12734385http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12734385
http://purl.uniprot.org/citations/12734385http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12734385
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