IndraLab

Statements

USP9X inhibits MCL1. 10 / 13
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"Downregulation of USP9x by siRNA in LNCaP cells prevented Mcl-1 stabilization, increased apoptosis induction and reduced clonogenic survival following irradiation, particularly in LNCaP but to a lesser extent also in PC3 cells."
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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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"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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"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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"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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"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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"McL-1 is one of the anti-apoptotic Bcl-2 protein family, which is reduced in islets in T1D patients, and USP9X modulates McL-1 protein turnover mediated by cytokines to prevent islet cell death in β cells (111)."
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"The interaction between TDRD3 and the ubiquitin-specific peptidase 9 X-linked (USP9X), which is dependent on arginine methylation of USP9X, prevents TDRD3 ubiquitination, together with a significant i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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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, 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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