IndraLab

Statements


Mutated USP8 leads to the deubiquitination of EGFR. 6 / 6
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"USP8 mutants diminished epidermal growth factor receptor ubiquitination and induced Pomc promoter activity in immortalized AtT-20 corticotropinoma cells."

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"USP8 mutations lead to enhanced deubiquitination of the epidermal growth factor receptor (EGFR) and result in an imbalance in EGFR signalling, accompanied by excessive activation of ACTH production and cell growth."

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"The cultured cells were transfected by mutant USP8 which was found to inhibit EGFR ubiquitination and degradation which increased the EGFR in the plasma membrane and returned to the cell surface by re[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Mutant USP8 inhibits EGFR ubiquitination and rescues it from proteasomal degradation, increasing the EGFR in the plasma membrane and returning to the cell surface by reversing the endocytosis and thus ultimately promoting ACTH secretion by activated EGFR signaling pathway (41)."

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"The identified USP8 mutants increase EGFR deubiquitination to inhibit EGF induced EGFR downregulation, leading to augmented and more sustained EGFR signaling."

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"The hyperactivated USP8 mutants enhanced the EGFR deubiquitination and protected it from degradation."