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- W1570774736 abstract "AACR Centennial Conference: Translational Cancer Medicine-- Nov 4-8, 2007; SingaporeB74 Epidermal Growth Factor Receptor (EGFR) is a known oncogene and malfunctioning of its receptor endocytosis and/or degradation may result in excessive signaling that could contribute to cancer transformation and tumorigenesis. Previously, we have identified Endofin, an endosomal protein, as one of the novel phosphoproteins from the analysis of an EGF-induced phosphotyrosine proteome using the cICAT-based LC-MS/MS method. Here we demonstrated that Endofin phosphorylation peaks at 30 minutes and starts to decrease after 1 hour. Further studies also showed that the localization of endofin to early endosomes is essential for its phosphorylation. This is indicated by the drastic decrease of Endofin phosphorylation in treated cells with wortmaninn, which prevents Endofin localization through inhibition of PI3P production. In addition, in vivo phosphorylation assay of Endofin FYVE mutant, C753S, resulted in drastic abolishment of phosphorylation, further supporting the notion that localization is crucial for phosphorylation. On the other hand, immunofluorescence staining of cells transfected with Endofin wild-type and phosphorylation site-mutants revealed that phosphorylation is not required for Endofin localization. All these results, taken together, suggest that endofin phosphorylation maybe important for its function at the early endsomes, such as regulation of EGFR endocytosis/degradation, which is a viable strategy in cancer therapeutics." @default.
- W1570774736 created "2016-06-24" @default.
- W1570774736 creator A5014257263 @default.
- W1570774736 creator A5036198629 @default.
- W1570774736 date "2007-11-15" @default.
- W1570774736 modified "2023-09-25" @default.
- W1570774736 title "Endofin is a novel component in EGF/EGFR oncogenic signaling" @default.
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