IndraLab

Statements


USP7 inhibits DNMT1. 8 / 9
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eidos
"Loss of USP7 enhances DNMT1 association with replication sites As increased histone ubiquitination is observed in USP7 KO cells , we next examined if loss of USP7 results in an increase of DNMT1 recruitment in S phase of cell cycle ."

reach
"Furthermore, loss of HAUSP combined with inhibition of HDAC activity had a synergistic effect on DNMT1 protein stability, because treatment of HAUSP knockout cells with various HDAC inhibitors reduced DNMT1 abundance to nearly undetectable amounts (XREF_FIG and XREF_SUPPLEMENTARY)."

reach
"USP7 enhanced DNMT1 activity, while USP7-siRNA inhibited DNMT1 functions and reduced the survival of MM cells [88]."

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"Expression of shRNA resistant wild-type Usp7 in Usp7 depleted cells reduced the size of Dnmt1 nuclear foci, but catalytically-inactive Usp7 (C223S) failed to do so."

eidos
"Thus , consistent with an increased DNA methylation phenotype , loss of USP7 apparently enhanced DNMT1 association with replicating DNA , a result consistent with a previous study44 ."

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"Deubiquitylating enzyme USP7 augmented DNMT1 functioning, while USP7-siRNA decreased DNMT1 function and reduced MM cell survival.Furthermore, RRx-001 plus USP7 inhibitor P5091 presented a synergistic effect against MM plasma cells."

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"It has been shown that acetylation of KG linker lysine residues impairs DNMT1USP7 interaction and promotes DNMT1 degradation [12]."

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"HDAC1 and HAUSP can prevent UHRF1 and DNMT1 from acetylation and ubiquitination for degradation mediated by Tip60 during S phase when the abundance of Tip60 is relatively low."