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USP9X activates MCL1. 31 / 41
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"We therefore investigated the effect of Usp9X knockdown in Mcl1 -/- MEFs to rule out the possibility that USP9X mediates its mitosis specific effects by stabilizing MCL1."
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"Taken together, BIX-01294 decreases the expression of USP9X and promotes the degradation of MCL1, which eventually leads to apoptosis in bladder cancer cells."
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"Conversely, USP9X is known to promote the activities of anti-apoptotic factors, MCL1 and Survivin."
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"Furthermore, the chemical inhibition of USP9X increased the sensitivity of the human lung carcinoma lines A549 and H1299 to an anti-apoptotic inhibitor (ABT-737, targets BCL-xl, but not MCL1)."
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"In Jurkat T lymphoma and K562 chronic myelogenous cells, USP9X is enzymatically activated in response to ionising radiation and causes MCL1 stabilisation, in turn inhibiting apoptosis and resulting in radioresistance [XREF_BIBR]."
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"Knockdown of USP9x increased Mcl-1 turnover but did not alter Mcl-1 mRNA levels, suggesting that the USP9x modifies Mcl-1 post-translationally."
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"USP9X mediates acute MCL-1 stabilization and protection from apoptosis in response to MAPK suppression caused by MEK inhibitors (113), which may provide a promising therapeutic strategy for pancreatic cancer."
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"USP9x knockdown enhanced radiation induced decrease of Mcl-1 and sensitized the radioresistant cells to apoptosis induction, whereas USP9x knockdown alone did not change Mcl-1 level in unirradiated cells."
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"Together, our results indicate that radiation induced activation of USP9x inhibits Mcl-1 degradation and apoptosis resulting in increased radioresistance."
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"For example, by stabilizing MCL1, USP9x can promote cancer cell survival or confer radioresistance in B-cell acute lymphoblastic leukemia [ 13 ], non-small-cell lung cancer [ 14 ] breast [ 15 ] and me[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In contrast, the deubiquitinase USP9x prevented Mcl-1 degradation and stabilized Mcl-1 levels by removing the poly-ubiquitin chain [XREF_BIBR]."
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"These data indicate that p300-dependent acetylation of MCL1 is critical for USP9X-mediated MCL1 stabilization, sensitizing cancer cells with relatively higher level of acetylated MCL1 to the USP9X inhibitor WP1130 (Figure 7)."
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"Importantly, examination of USP9X targets MCL1 and beta-catenin by western blot analysis did not reveal a change in their protein levels when USP9X was knocked down in DAOY cells."
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"Conversely , knockdown or therapeutic targeting of USP9X destabilizes MCL-1 and sensitizes tumor cells to BCL-2 / BCL-xL inhibitors [ 36 , 43 ] ."
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"Usp9X inhibition depletes Mcl-1 Based on our previously published observation that Usp9X induces a decline of Mcl-1 protein levels in GBM cells9 ,11 , we hypothesized that similar effects would be observed in MPNST cells ."
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"USP9X has been shown to promote Mcl-1 stabilization and to increase tumor cell survival in response to radiation and chemotherapy in several tumor types (19, 36–39)."
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"For example, by removing K48 linked polyubiquitin chains from MCL1, USP9X inhibits the proteasomal degradation of MCL1, a pro survival BCL2 family member that is overexpressed in multiple cancer types and contributes to chemoresistance and tumor recurrence [XREF_BIBR]."
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"USP9x expression correlated moderately but significantly with Mcl-1 expression in glioblastoma, supporting our hypothesis that USP9x stabilizes Mcl-1 in glioblastoma cells."
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"In addition, ionising radiation induced activation of USP9x inhibits Mcl-1 degradation, resulting in increased radio-resistance and apoptosis [XREF_BIBR]."
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"Usp9X inhibition depletes Mcl-1."
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"USP9X prolongs the half-life of MCL1 in an enzymatic activity-dependent manner by specifically cleaving the degradative K48-linked chains on MCL1 to prevent its proteasomal degradation ."
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"This result indicates that the inhibition of USP9X accelerates Mcl-1 degradation and hence that USP9X activities are critical for Mcl-1 stability."
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"Recent reports have suggested also that USP9X enhances Mcl-1 stability by preventing its proteasomal destruction through de-ubiquitination [XREF_BIBR]."
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"Knockdown of USP9X results in downregulation of MCL1 , which enhances cell apoptosis in human follicular lymphomas and B-cell lymphomas [ 123 ] ."
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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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"Finally, we want to point out that our experiments analyzing USP9x-mediated Mcl-1 stability were carried out in two prostate cancer cell lines only."
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"Our data revealed that USP9x increased the protein stability of anti-apoptotic Mcl-1, resulting in the accumulation of the protective protein, particularly in LNCaP cells."
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"Recently, downregulation of usp9x was shown to inhibit tumor cell growth by promoting cyclin D1 and MCL-1 degradation, respectively, suggesting that silencing of specific DUBs in tumor cells may be an[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Peddaboina et al. also found that USP9X inhibition downregulated MCL1, an anti-apoptotic factor in the BCL2 (BCL2, apoptosis regulator) gene family, thereby increasing the sensitivity of solid tumor cells to various chemotherapeutic agents, including Bcl-2/Bcl-XL inhibitors."
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"Downregulating USP9X increased tumor sensitivity to chemotherapy by degrading the MCL1 protein [31]."
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"USP9X has, however, also been proposed to promote tumor cell survival by limiting the degradation of the anti-apoptotic protein Mcl-1."
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