IndraLab

Statements

USP28 activates FBXW7. 10 / 10
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"This result suggests that Usp28 preferentially stabilizes Fbw7 due to more efficient binding and is consistent with the idea that Fbw7 targets Usp28 to its substrates.We concluded that stabilization o[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In several tissues, including lung, liver and pancreas, deletion of Usp28 downregulates Fbw7 and promotes accumulation of its substrates."
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"In contrast, complete absence of Usp28 triggers autocatalytic turnover of Fbw7 and leads to Fbw7 substrate stabilization.The most likely explanation for such nonlinear pattern of regulation is that Fb[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Preferential targeting of Fbw7 by Usp28 shifts the default activity of this system toward Fbw7 substrate ubiquitination and provides a mechanism to maintain physiological levels of multiple proto-onco[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Knockout of Usp28 triggered Fbw7 degradation and accumulation of Fbw7 substrates, resulting in oncogenic transformation."
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"In addition, FBXW7 induced degradation of MYC is fine tuned by the de-ubiquitylation enzyme USP28 [XREF_BIBR], which slows down poly-ubiquitylation, as well as by the E3 ligase betaTRCP, which counteracts FBXW7 by conjugating mixed Ub chains to MYC that disfavors degradation."
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"USP28, a deubiquitinating enzyme, causes BRAF degradation by stabilizing FBXW7 [29]."
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"In agreement with this hypothesis, treatment of Usp28 -/- MEFs with PiB, a specific Pin1 inhibitor, attenuated degradation of ectopic Fbw7."
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"Similarly, USP28 prevents FBXW7 self-degradation in chronic lymphocytic leukemia (CLL), leading to elevated levels of Notch1 (Close et al., 2018)."
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"Intriguingly, deletion of Usp28 also suppresses intestinal tumor development in the absence of Fbw7, possibly via Fbw7-independent regulation of substrates like Notch, Jun and Myc [102] ."
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