IndraLab

Statements

EGFR activates USP8. 11 / 11
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"EGFR activates USP8 by phosphorylating Tyr 717 and Tyr 810."
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"Taken together, EGFR activates USP8 by directly phosphorylating Tyr 717 and -810 in vitro."
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"Most importantly, epidermal growth factor receptor (EGFR) kinase activated USP8 by phosphorylating Tyr 717 and Tyr 810."
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"Importantly, GST-EGFR phosphorylated non-tagged USP8 and elevated its DUB activity toward ubiquitin oligomers (Fig.  xref ; lanes 1–3), but GST-EGFR did not activate GST-USP8 (Supplementary Fig.  xref )."
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"EGFR activation causes USP8 to become phosphorylated and to associate with EGFR on endosomes where it dynamically regulates EGFR ubiquitination state during trafficking."
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"Upon binding to epidermal growth factor (EGF), EGF receptor kinase phosphorylates and activates USP8 [ 102 ], which in turn deubiquitinates TCHP to counteract its ubiquitination by CRL3 KCTD17 [ 43 ]."
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"Taken together, EGFR activates USP8 by directly phosphorylating Tyr-717 and −810 in vitro."
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"EGFR activates USP8 by phosphorylating Tyr-717 and Tyr-810.|Here, we report that epidermal growth factor receptor (EGFR) kinase suppresses ciliogenesis by directly phosphorylating the deubiquitinase USP8 on Tyr 717 and Tyr 810 in RPE1 cells."
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"EGFR activates USP8 by phosphorylating Tyr-717 and Tyr-810."
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"We also demonstrated that USP8 was activated by EGFR tyrosine kinase through phosphorylation of Tyr717 and Tyr810."
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"EGFR activates USP8 by phosphorylating Tyr-717 and Tyr-810.|Here, we report that epidermal growth factor receptor (EGFR) kinase suppresses ciliogenesis by directly phosphorylating the deubiquitinase USP8 on Tyr 717 and Tyr 810 in RPE1 cells."
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