IndraLab

Statements

USP9X inhibits MCL1. 7 / 10
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"Given that Noxa is an inhibitor of Mcl-1 and has been known to stimulate Mcl-1 mediated proteasomal degradation, Usp9X inhibition might in part lead to a reduction of Mcl-1 levels through Noxa mediated destabilization of Mcl-1."
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"Indeed, knock-down of USP9X reduced the half-life of Mcl-1 and increased its conjugation to Lys48 linked poly-ubiquitin chains [XREF_BIBR] that generally target proteins for proteasomal degradation."
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"This may explain why WP1130, but not USP9x knockout, abrogated the MCL-1i induced stability of Mcl-1 protein."
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"Indeed, knockdown of Usp9X increased mitotic cell death in Mcl1 -/- cells to a similar extent as in WT MEFs, thus indicating independence of MCL1 (Fig XREF_FIG A and B)."
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"The USP9X inhibitor WP1130 or depletion of USP9X by its specific shRNAs induces MCL-1 degradation in cells and increases tumor cell sensitivity to chemo and radiotherapies 39."
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"Although USP9X depletion did not cause an obvious change in Mcl-1 degradation during mitosis, it did increase the loss of other mitotic APC/C substrates, in particular cyclin A, but also cyclin B and NEK2A (XREF_FIG A)."
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"Therefore, the indirectly supported, USP9X mediated degradation of MCL-1 can be regarded as a novel autophagy independent, oncosuppressive function of BECLIN 1 [XREF_BIBR]."
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