IndraLab

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USP7 activates Ubiquitin. 18 / 20
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"The specificity of SJB was confirmed by various experiments : first, we show that SJB potently and selectively block USP1 activity without inhibiting other DUBs (USP2/USP5/USP7/USP14/UCH37); second, SJB inhibited binding of USP1 with HA-Ub-VS probe, but it did not affect labeling of other DUBs with probe; and third, SJB inhibited USP1, but not USP2 or USP7, triggered cleavage of ubiquitin tetramer chains."
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"USP7 deubiquitinase promotes ubiquitin dependent DNA damage signaling by stabilizing RNF168."
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"They include the potential recruitment of DUBs for the stabilization of beta-catenin in Epstein-Barr virus (EBV)-infected B cells, and the specific targeting of the cellular DUB ubiquitin specific protease 7 (USP7) by the Epstein-Barr nuclear antigen 1 (EBNA1) and the herpes simplex virus type 1 (HSV-1) regulatory protein ICP0."
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"These results suggest that the USP7-mediated deubiquitylation couples the completion of DNA methylation by DNMT1.Failure of DNA methylation replication has been shown to be accompanied by accumulation of UHRF1 on chromatin and enhanced UHRF1-dependent ubiquitin signaling."
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"The USP7 gene, located on chromosome 16p13.2, encodes for a deubiquitinase, enabling the removal of ubiquitin molecules from target proteins (Hao et al., 2015; Fountain et al., 2019; van der Laan et al., 2023; Wimmer et al., 2024)."
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"These compounds may selectively interfere with K48 linkage-directed ubiquitin chain cleavage mediated by USP7, suggesting that K48-linked substrates such as MDM2 could be susceptible."
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"USP7 prevents HLTF degradation via the ubiquitin‐proteasome pathway to upregulate the downstream expression of SLC7A11, ultimately inhibiting ferroptosis in GBM cells (Figure 9)."
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"Usp7 is thought to exist in equilibrium between inactive and active forms, and its activity is enhanced allosterically by the metabolic enzyme, GMPS, which binds and activates the HUBL domain of Usp7, increasing the ubiquitin binding and catalytic activity of Usp7 by 100-fold."
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"Within tumor inflammation, USP7 modulates tumor growth and immune responses by removing ubiquitin tags from key proteins, thereby altering their stability and function [4]."
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"HAUSP enhances Mdm2 stability by removing ubiquitin moieties from Mdm2 ( Li et al., 2004; Meulmeester et al., 2005 )."
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"Mechanistically, USP7 interacts with SMAD2/3, enhancing their protein stability by removing the K48 ubiquitin chain from both proteins and preventing their proteasome degradation, thus increasing the p-SMAD2 levels and nuclear entry."
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"In much the same way that NF-κB can have both tumour promoting or suppressing roles depending on the cellular context [1,30–33], DUBs such as USP7 can elicit its effects by removing ubiquitin moieties from both tumour suppressor proteins such p53 [34] and oncogenes such as c-Myc [35]."
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"We hypothesized and verified the conjecture that USP7 mediates the stability of ARF4 by removing the Lys-48-linked Ub chain, but not the Lys-63-linked Ub chain."
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"First, we tested whether USP7 could stimulate p53 function in a ubiquitin independent manner during conditions of cellular stress such as DNA damage."
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"Regulation of USP7 by viruses may enable fine tuning of ubiquitin signals on targeted cellular proteins and may indirectly affect damage responses."
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"Indeed, such effects were reported for HAUSP mediated ubiquitin removal of PTEN (phosphatase and tensin homologue deleted in chromosome 10) and FOXO (Forkhead box O) 4."
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"Leger and co-workers [80] produced a cluster of selective and orally bioavailable ubiquitin-specific protease 7 (USP7) inhibitors based on the structure of existing inhibitors."
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"However, it is currently unknown whether there is a functional interaction between UAF1–USP1, USP7, USP11, and ATAD5 that leads to Ub–PCNA deubiquitination.We have previously reported that ATAD5–RLC can unload mono-Ub or poly-Ub–PCNA from DNA (46)."
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