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USP7 binds DAXX and MDM2. 45 / 45
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"We investigated whether berberine, like doxorubicin, induces a similar disruption of the MDM2, DAXX, and HAUSP complex."
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"A recent report showed that berberine can up-regulate p53 by disrupting the MDM2-DAXX-HAUSP interactions and promoting MDM2 self-ubiquitination and degradation xref ."
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"The MDM2-DAXX-HAUSP interactions were also rapidly disrupted in berberine-treated cells, so a similar reduction of MDM2 as was seen in doxorubicin-treated cells appeared to occur ( xref )."
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"Several compounds inhibit MDM2 interaction with other molecules, such as berberine which disrupts the MDM2, DAXX, and HAUSP complex XREF_BIBR."
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"MDM2, a negative regulator of p53 normally associated with DAXX and HAUSP to form MDM2-DAXX-HAUSP complex [12]."
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"Because berberine induced a similar disruption of the MDM2, DAXX, and HAUSP complex as did doxorubicin, the question raised was why berberine induced a persistent degradation of MDM2, whereas doxorubicin only induced a transient downregulation of MDM2 that was followed by an increase in MDM2 expression."
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"The persistent self-ubiquitination of MDM2 in the berberine-treated cells was found to be due to the lack of formation of a new MDM2-DAXX-HAUSP complex."
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"In further studies, we demonstrated that berberine uniquely downregulated the expression of DAXX in a dose- and time-dependent manner, and because of that DAXX absence in berberine-treated cells, no new formation of the MDM2-DAXX-HAUSP complex was possible, so the p53-induced newly-synthesized MDM2 constitutively underwent self-ubiquitination and degradation."
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"MDM2, a prominent antagonist of p53 regulates its expression in cancer cells and remains associated with DAXX and HAUSP to form MDM2-DAXX-HAUSP complex."
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"In unstressed cells, MDM2 interacts with DAXX and HAUSP and is stabilized in the MDM2, DAXX, and HAUSP complex, which leads to persistent ubiquitination and degradation of the tumor suppressor p53."
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"Trisenox disrupts MDM2- DAXX-HAUSP complex."
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"In unstressed cells, DAXX interacts with USP7 and MDM2, and mediates the stabilization of USP7 on MDM2, thus blocking p53 activation."
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"Under conditions of cellular stress and DNA damage, such when challenged with doxorubicin (XREF_SUPPLEMENTARY), MDM2 becomes dissociated from the MDM2, DAXX, and HAUSP complex resulting in instability, as MDM2 self ubiquitination and degradation occur."
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"We believe that discovery of drugs to target MDM2 by disrupting the MDM2-DAXX-HAUSP interaction is an innovative concept in the development of therapies for cancer patients whose neoplastic cells overexpress MDM2."
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"In further studies, we demonstrated that berberine uniquely downregulated the expression of DAXX in a dose- and time dependent manner, and because of that DAXX absence in berberine treated cells, no new formation of the MDM2, DAXX, and HAUSP complex was possible, so the p53 induced newly synthesized MDM2 constitutively underwent self ubiquitination and degradation."
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"The association of RASSF1A with MDM2 after DNA damage, disrupts MDM2’s interaction with DAXX and HAUSP proteins, leading to MDM2 ubiquitination, thus promoting the stabilization and activation of p53 xref , xref ."
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"XREF_BIBR, XREF_BIBR Clinical trials of Trisenox (arsenic trioxide), which is used for treatment of acute promyelocytic leukemia (APL), disrupts the MDM2, DAXX, and HAUSP complex (reported at AACR 2016)."
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"Song et al. [20] recently showed that, in response to DNA damage, RASSF1A promotes the disruption of the MDM2, DAXX, and HAUSP complex, which results in MDM2 self ubiquitination, p53 stabilization, an[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"It has been reported that RASSF1A negatively regulates MDM2 by disrupting the MDM2, DAXX, and HAUSP complex and inducing the self ubiquitination of MDM2 [XREF_BIBR]."
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"RASSF1A has been reported to control the assembly of the USP7, DAXX, and MDM2 complex by blocking interactions among MDM2, DAXX and USP7, and by promoting the ubiquitination of MDM2, resulting in stabilization of p53."
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"The RASSF1A tumor suppressor is one such protein, which disrupts the Mdm2-DAXX-USP7 interaction in response to DNA damage by simultaneously binding to both Mdm2 and DAXX."
32850836
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"In unstressed cells, Daxx binds simultaneously to Mdm2 and the deubiquitinase Hausp (herpesvirus-associated ubiquitin-specific protease; also known as USP7), mediating the stabilizing effect of Hausp on Mdm2 xref ."
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"The activity of HAUSP towards Mdm2 can further be enhanced by the DAXX protein, which binds simultaneously to Mdm2 and HAUSP (Tang, J. et  al., 2006)."
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"DAXX and HAUSP interact with MDM2 to form a tertiary complex, which reduces self-ubiqitination of MDM2 [ xref ]."
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"Berberine also decreases DAXX transcription, and subsequently prevents the formation of the MDM2-DAXX-HAUSP complex, resulting in the persistent self-ubiquitination of MDM2 in ALL cells [ xref ]."
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"It is further discovered that berberine also decreases DAXX expression at the transcriptional level, and subsequently prevents the formation of the MDM2-DAXX-HAUSP complex, resulting in the persistent self-ubiquitination of MDM2 in ALL cells [ xref ]."
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"Recent studies demonstrated that MDM2, DAXX and HAUSP interact with each other to form a tertiary complex."
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"The tumour suppressor RASSF1A promotes MDM2 self ubiquitination by disrupting the MDM2, DAXX, and HAUSP complex."
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"DNA damage would disrupt the MDM2, Daxx, and HAUSP complex, resulting in increased MDM2 degradation and p53 stabilization."
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"RASSF1A promotes MDM2 self ubiquitination and p53 stabilization by disrupting the MDM2, DAXX, and HAUSP complex in the nucleus [72]."
33445626
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"RASSF1A disrupts the interaction between Mdm2, DAXX, and HAUSP, thereby promoting Mdm2 ubiquitination, and consequently resulting in p53 stabilization."
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"We discovered that downregulation of MDM2 in ALL cells by berberine occurred at a post-translational level through modulation of DAXX, which disrupted the MDM2-DAXX-HAUSP interactions and thereby promoted MDM2 self-ubiquitination and degradation."
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"The dynamics of the Mdm2, Daxx, and Hausp complex underscore its importance in the p53 pathway."
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"An important function of Daxx is the regulation of p53 mediated apoptosis via cooperation with a Daxx, Axin, Hipk2, and p53 complex 49 and the DNA-damage-dependent dissociation of the Mdm2, Daxx, and Hausp complex."
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"The anti-cancer drugs, doxorubicin and VP-16 act inside cancer cells by successfully disrupting the MDM2, DAXX, and HAUSP complex and degrading MDM2 expression XREF_BIBR."
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"In the absence of DNA damage, the DAXX protein binds to USP7 and HDM2, facilitating the HDM2 deubiquitination ( xref )."
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"Berberine increases MDM2 self-ubiquitination by disrupting MDM2-DAXX-HAUSP interactions."
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"RASSF3 interacts with MDM2 via SARAH domain [XREF_BIBR], while RASSF1A promotes MDM2 self ubiquetination by disrupting the MDM2, DAXX, and HAUSP complex, resulting in the stabilization and activation of p53 [XREF_BIBR]."
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"Importantly, we also found that the disruption of MDM2-DAXX-HAUSP interactions resulted in enhanced MDM2 ubiquitination ( xref )."
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"It has been demonstrated that DAXX interacts with MDM2 and HAUSP (herpes virus-associated ubiquitin-specific protease) to form a tertiary complex."
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"The tumour suppressor RASSF1A promotes MDM2 self ubiquitination by disrupting the MDM2, DAXX, and HAUSP complex."
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"By the same concept, interaction of Daxx and DENVC in the nucleus may disrupt the Mdm2, Daxx, and Hausp complex leading to degradation of Mdm2 by self ubiquitination, accumulation of p53 and sensitiza[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In unstressed cells, MDM2 interacts with DAXX and HAUSP and is stabilized in the MDM2-DAXX-HAUSP complex, which leads to persistent ubiquitination and degradation of the tumor suppressor p53."
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"The natural product berberine can induce MDM2 degradation through disrupting the MDM2-DAXX-HAUSP interaction ( xref )."
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"In the presence of intact DAXX and HAUSP, the newly synthesized MDM2 could associate with DAXX and HAUSP again, leading to stabilization of MDM2 and new ubiquitination and degradation of p53."
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