IndraLab

Statements


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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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"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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"Here we present structural, biochemical, and biophysical analyses elucidating the molecular mechanism by which the C-terminal 19 amino acids of USP7 (residues 1084-1102) enhance the ubiquitin cleavage activity of the deubiquitinase (DUB) domain."

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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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"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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"USP7 deubiquitinase promotes ubiquitin dependent DNA damage signaling by stabilizing RNF168."

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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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"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."