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- W3164417147 abstract "FBXW7 acts as a typical tumor suppressor, with loss of function alterations in human cancers, by promoting ubiquitylation and degradation of many oncoproteins. Lysine-specific demethylase 1 (LSD1) is a well-characterized histone demethylase. Whether LSD1 has demethylase-independent activity remains elusive. Here we report that LSD1 directly binds to FBXW7 to destabilize FBXW7 independent of its demethylase activity. Specifically, LSD1 is a pseudo-substrate of FBXW7 and LSD1-FBXW7 binding does not trigger LSD1 ubiquitylation, instead promote FBXW7 self-ubiquitylation by preventing FBXW7 dimerization. The self-ubiquitylated FBXW7 is subjected to degradation by proteasome and lysosome in a manner dependent of autophagy protein p62/SQSTM1. Biologically, LSD1 destabilizes FBXW7 to abrogate its functions in growth suppression, NHEJ repair and radioprotection. Collectively, our study revealed a previously unknown activity of LSD1, which likely contributes to its oncogenic function. Targeting LSD1 protein, rather than its demethylase activity, might be a unique approach for LSD1-based drug discovery for anti-cancer application." @default.
- W3164417147 created "2021-06-07" @default.
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- W3164417147 date "2018-01-01" @default.
- W3164417147 modified "2023-09-23" @default.
- W3164417147 title "LSD1 Destabilizes FBXW7 Independent of Its Demethylase Activity" @default.
- W3164417147 doi "https://doi.org/10.2139/ssrn.3281653" @default.
- W3164417147 hasPublicationYear "2018" @default.
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