IndraLab

Statements


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"In EGF stimulated cells, UBPY underwent ubiquitination and bound to EGFR."

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"UBPY binds to endocytosed EGFR and deubiquitinates it on early endosomes [10] ."

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"However, the level of UBPY S680A binding to EGFR was comparable to that of wild-type UBPY ( Supplementary Fig. S2 )."

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"When overexpressed in HeLa cells, USP8 mutations were associated with reduced EGFR ubiquitination and degradation as compared to WT controls."

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"We therefore examined whether the binding of UBPY to EGFR is indirect and mediated by 14-3-3 proteins which normally exist as a dimer [18]."

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"We therefore examined whether the binding of UBPY to EGFR is indirect and mediated by 14-3-3 proteins which normally exist as a dimer [18] ."

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"In EGF-stimulated cells, UBPY underwent ubiquitination and bound to EGFR."

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"Overall, these results support and extend our previous model that Usp8 and EGFR associate via multiple molecular interactions."

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"Immunoblotting of the precipitates with anti-FLAG antibody showed that wild-type UBPY and UBPY S680A bind to EGFR with similar efficiency upon EGF stimulation ( Supplementary Fig. S2 ), indicating th[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"By conducting an Immunoprecipitation assay, we found an interaction between endogenous USP8 and EGFR in both cell lines, confirming that EGFR is a USP8 's client protein (XREF_FIG)."

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"Furthermore, we demonstrate that optimal Usp8 tyrosine phosphorylation is not necessary for binding of Usp8 to EGFR."

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"The percentage of EGFR-positive tumors was much lower in our cohort than in a published cohort, in which USP8 mutations were associated with higher EGFR expression [ xref ]."

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"We have previously shown that UBPY binds and deubiquitinates ligand-activated EGFR at early endosomes [10] ."

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"This finding extends our previous observations that Usp8 is tyrosine phosphorylated upon stimulation of the EGFR and that Usp8 is recruited to the EGFR via multiple interactions including (direct) bin[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"It is not clear why the data of XREF_BIBR showed an opposite effect on EGFR by USP8, but it is supported by their observations that upon EGF stimulation, USP8 directly binds EGFR."

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"On the other hand, 14-3-3zeta has been reported to bind ligand activated EGFR [25], raising the possibility that the interaction between UBPY and activated EGFR is mediated by the 14-3-3 dimer."

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"USP8 interacts with the epidermal growth factor receptor, and regulates proliferation and differentiation."

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"Immunoblotting of the precipitates with anti-FLAG antibody showed that wild-type UBPY and UBPY S680A bind to EGFR with similar efficiency upon EGF stimulation, indicating that the interaction between [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Because USP8 has been reported to regulate a number of cancer targets including EGFR, xref – xref we first explored whether USP8 might interact with EGFR in NSCLCs, H1299 and H1650 cells."

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"By conducting an Immunoprecipitation assay, we found an interaction between endogenous USP8 and EGFR in both cell lines, confirming that EGFR is a USP8’s client protein ( xref )."

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"Furthermore, mutation of S680 resulted in enhanced Usp8 activity towards EGFR, although the EGFRUsp8 interaction itself was not affected by S680 mutation."

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"USP8 interacts with many substrates such as the epidermal growth factor receptor, an essential regulator of proliferation and differentiation, and regulates endosomal trafficking by ubiquitin-mediated sorting of the endocytosed cargoes ( xref ; xref ; xref )."