IndraLab

Statements

EGFR phosphorylates USP8. 9 / 9
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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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"EGFR phosphorylates the ubiquitinase USP8, which stabilizes the trichoplein–Aurora A pathway and suppresses ciliogenesis."
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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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"To validate the effect of EGFR phosphorylation of USP8 in vitro, we used also non tagged USP8 because GST-USP8 had a significantly higher DUB activity than non tagged USP8 in non phosphorylated forms."
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"Overall, we have provided strong evidence for ligand-induced ERBB- and SRC family kinase-dependent tyrosine phosphorylation of Usp8 1–504."
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"To validate the effect of EGFR phosphorylation of USP8 in vitro, we used also non-tagged USP8 because GST-USP8 had a significantly higher DUB activity than non-tagged USP8 in non-phosphorylated forms (Supplementary Fig.  xref )."
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"Recently, it has been reported that EGFR suppresses ciliogenesis by directly phosphorylating the deubiquitinase USP8 in RPE1 cells [86]."
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"Among these, Usp8/UbpY interacts with and is phosphorylated by activated epidermal growth factor receptor (EGFR), but its precise function in EGFR-signaling remains to be established."
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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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