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• W2116718922 abstract "c-Cbl associates with the activated EGF receptor before endocytosis. We here reveal that the capacity of c-Cbl to promote receptor internalization depends on its ubiquitin ligase activity, which functionally connects the EGF receptor to Eps15, a mediator of clathrin-coated pit formation. EGF-induced phosphorylation of Eps15, as well as recruitment of Eps15 to the plasma membrane and its co-localization with the EGF receptor in endosomes required the ubiquitin ligase activity of c-Cbl. This suggested that ubiquitin provides a direct or indirect link between the receptor and Eps15. Indeed, EGF-induced redistribution of Eps15 to the plasma membrane and endosomes depended on its ubiquitin-interacting motif. Upon over-expression, the ubiquitin-interacting motif abrogated the capacity of c-Cbl to promote EGF receptor endocytosis and only allowed receptor internalization via a route that lacked Eps15. Our findings disclose a novel function for the c-Cbl ubiquitin ligase and identify ubiquitin as a module that directs the EGF receptor into an endocytic pathway involving Eps15." @default.
• W2116718922 created "2016-06-24" @default.
• W2116718922 creator A5013783474 @default.
• W2116718922 creator A5081990233 @default.
• W2116718922 creator A5084635195 @default.
• W2116718922 date "2004-10-01" @default.
• W2116718922 modified "2023-10-10" @default.
• W2116718922 title "c-Cbl directs EGF receptors into an endocytic pathway that involves the ubiquitin-interacting motif of Eps15" @default.
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• W2116718922 doi "https://doi.org/10.1242/jcs.01354" @default.
• W2116718922 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15383614" @default.
• W2116718922 hasPublicationYear "2004" @default.
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