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USP7 activates DNMT1. 20 / 25
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"Therefore, the DNA substrate was used in large excess (3-to 24-fold molar ratio), suggesting that USP7 modulates Dnmt1 's enzymatic activity rather than acting as a recruitment factor."
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"In one study , USP7 was shown to stimulate DNMT1 activity in vitro and knockdown of USP7 reduced the levels of DNA methylation on several silenced genes39 ."
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"78 DNMT1, which is frequently overexpressed in cancers, is rescued by HAUSP from UHRF1 mediated ubiquitination."
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"Thus, the environment provided by USP7 greatly affects the intrinsic dynamics of DNMT1, supporting the experimental results that the intermolecular interactions are required for USP7-mediated stabilization of DNMT1 [15]."
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"Interestingly, binding of USP7 also increased the activity of DNMT1 in vitro, indicating that USP7 acts as a general positive factor of DNMT1, by increasing the stability and activity of the methyltransferase."
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"A caveat in this experiment is that , given the observed interaction between USP7 and DNMT1 , depletion of USP7 would also reduce DNMT1 and thus impaired DNA methylation ."
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"Although the inter-molecular interaction is considered to be required for USP7-mediated stabilization of DNMT1, the detailed allosteric regulation caused by USP7 still needs to be answered.Through mapping to the DNMT1 structure, 13 mutations occur in the RFTS domain (Figure 1C), which are important for the enzymatic activity, function, and subcellular localization of DNMT1 [3]."
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"Molecular mechanism for USP7 mediated DNMT1 stabilization by acetylation."
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"Among those identified were DNMT1, RAE1, Bub3 and Nup98, the stability and functions of which are potentially regulated by Hausp."
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"USP7 regulates the stability of UHRF1 via its deubiquitylase activity [Felle et al., 2011; Qin et al., 2011; Ma et al., 2012], and modulates the enzymatic activity of Dnmt1 on the UHRF1 platform [Bostick et al., 2007; Sharif et al., 2007; Felle et al., 2011; Qin et al., 2011]."
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"Furthermore, reconstitution of HAUSP expression in knockout cells restored DNMT1 abundance to an extent comparable to that in parental cells (XREF_FIG), suggesting that loss of HAUSP is the sole cause of DNMT1 instability."
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"For instance, the loss of HAUSP in colorectal cancer cells potentiates apoptotic cell death by inducing proteasomal degradation of DNMT1, further compounding the potential of HAUSP inhibition as an effective anti-cancer therapy XREF_BIBR - XREF_BIBR."
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"The deubiquitylating enzyme USP7 is known to stimulate the DNMT1 activity, and conversely, USP7-siRNA reduces DNMT1 activity and decreases tumor cell viability [XREF_BIBR]."
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"Of note, targeting USP7-mediated DNMT1 stabilisation in pancreatic cancer holds distinct promise as therapeutic application."
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"Deubiquitylating enzyme USP7 stimulates DNMT1 activity; and conversely, USP7-siRNA reduced DNMT1 activity and decreased MM cell viability."
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"Next, we studied whether USP7 inhibition enhances activity of RRx-001 by triggering a more pronounced decrease in DNMT1 activity."
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"Besides, USP7 targets the proteins of the FOXO family in lung cancer and DNMT1 in colon cancer and acts as a deubiquitinase for SUMO (small ubiquitin like modifier) [XREF_BIBR]."
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"Deubiquitylating (DUB) enzyme USP7 stimulates DNMT1 activity and blockade of USP7 enhances anti-MM activity of RRx-001."
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"Overall, our studies provide new insights into the acetylation regulated and USP7 mediated stabilization of DNMT1."
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"The deubiquitylating enzyme USP7 stimulates DNMT1 activity, and conversely, USP7-siRNA reduced DNMT1 activity and decreased MM cell viability."
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