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• W2079244398 startingPage "2407" @default.
• W2079244398 abstract "Overexpression of ErbB-2/HER2 is associated with aggressive human malignancies, and therapeutic strategies targeting the oncoprotein are currently in different stages of clinical application. Tyrosine kinase inhibitors (TKIs) that block the nucleotide-binding site of the kinase are especially effective against tumors. Here we report an unexpected activity of TKIs: along with inhibition of tyrosine phosphorylation, they enhance ubiquitylation and accelerate endocytosis and subsequent intracellular destruction of ErbB-2 molecules. Especially potent is an irreversible TKI (CI-1033) that alkylates a cysteine specific to ErbB receptors. The degradative pathway stimulated by TKIs appears to be chaperone mediated, and is common to the heat shock protein 90 (Hsp90) antagonist geldanamycin and a stress-induced mechanism. In agreement with this conclusion, CI-1033 and geldanamycin additively inhibit tumor cell growth. Based upon a model for drug-induced degradation of ErbB-2, we propose a general strategy for selective destruction of oncoproteins by targeting their interaction with molecular chaperones." @default.
• W2079244398 created "2016-06-24" @default.
• W2079244398 creator A5048298854 @default.
• W2079244398 date "2002-05-15" @default.
• W2079244398 modified "2023-10-06" @default.
• W2079244398 title "Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy" @default.
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• W2079244398 doi "https://doi.org/10.1093/emboj/21.10.2407" @default.
• W2079244398 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/126014" @default.
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