IndraLab

Statements


USP9X deubiquitinates MCL1. 24 / 24
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"USP9X deubiquitinates and stabilizes MCL1 in distinct human cancers including human follicular lymphomas, diffuse large B cell lymphomas, glioblastoma, colon and lung cancers 19."

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"Conversely, ubiquitination of Mcl1 can be reversed by the deubiquitinase USP9X and the more recently identified USP13 ."

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"USP9X interacts with and deubiquitinates MCL-1, thereby stabilising it."

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"It has been reported that Usp9x deubiquitinates Mcl-1 by removing the conjugated ubiquition."

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"The overexpression of USP9X stabilizes the MCL1 protein in human lymphomas, and the depletion of USP9X increases MCL1 ubiquitination, which leads to MM cell apoptosis [31]."
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"In that study, USP9X, but not a catalytically inactive form of USP9X, was shown to decrease MCL1 ubiquitination in vitro."

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"Previous studies showed that USP9X deubiquitinates MCL1 and promotes cancer cell survival in human follicular lymphomas and diffuse large B cell lymphomas 19."

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"USP9X deubiquitinates and stabilizes MCL-1, a pro survival BCL2 family member XREF_BIBR, whose overexpression is associated with several neoplastic conditions XREF_BIBR - XREF_BIBR."

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"Disruption of Mcl-1:Noxa interaction followed by Noxa degradation, enhanced Mcl-1 de-ubiquitination by USP9x, and Mule destabilization are the major effects of these inhibitors."

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"USP9X deubiquitylation of MCL1 inhibits its proteasomal degradation, thus promoting its anti-apoptotic functions."

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"We next looked at expression levels of regulators of MCL-1 polyubiquitination and focused on USP9X, which deubiquitinates and stabilizes MCL-1 ."

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"Mechanistically, acetylation of MCL1 resulted in enhanced interaction with USP9X, which, in turn, promotes USP9X-dependent MCL1 deubiquitination."

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"Deubiquitination of Mcl-1 by USP9X."

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"USP9X deubiquitylates poly-ubiquitylated MCL1, protecting it from proteasomal degradation, thus increasing its stability and thereby promoting cell survival."

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"Conversely, the deubiquitinase USP9X reverses polyubiquitination of Mcl-1 and promotes its stability [XREF_BIBR]."

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"Thus in multiple cancer cell types, the level at which USP9X is able to deubiquitylate and stabilise MCL1 dictates its anti-apoptotic function."

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"Two DUBs USP9X and USP13 deubiquitinate and stabilise MCL1, and hypomorphic mutations in both have been linked to neurodevelopmental disorders and neurodegenerative disease [XREF_BIBR, XREF_BIBR]."

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"USP9X can deubiquitinate and stabilize MCL1, a protein essential for the survival of stem and progenitor cells from multiple lineages, thereby promoting cell survival."

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"Interestingly, knockdown of USP9x increases MCL-1 ubiquitination and turnover."

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"The inhibition of USP9x should increase the ubiquitination of Mcl-1."

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"XREF_BIBR, XREF_BIBR, XREF_BIBR In addition, a recent study showed that de-ubiquitinase USP9X inhibits Mcl-1 ubiquitination, thereby stabilizing protein levels and promoting tumor cell survival."

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"USP9X also deubiquitinated Mcl-1 in vitro, and generated free mono-ubiquitin [XREF_BIBR]."

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"For example, USP1 deubiquitinates two critical DNA repair proteins, FANCD2 and PCNA, and is therefore involved in Fanconi leukemia XREF_BIBR, XREF_BIBR; USP9x deubiquitinates and stabilizes the pro survival protein MCL1, and a correlation between USP9x expression and MCL1 levels was reported in human follicular lymphomas and diffuse large B-cell lymphomas 84; USP37 is a deubiquitinase regulating cell cycle by deubiquitinating cyclin A 85 and c-MYC 86."