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USP7 deubiquitinates DNMT1. 12 / 12
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"The UHRF1 and DNMT1 complex has been reported to contain USP7 that deubiquitinates and stabilizes DNMT1 XREF_BIBR, XREF_BIBR."

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"Recent evidence has indicated that USP7 also deubiquitinates DNMT1 during S-phase; in late S-phase, acetylation of DNMT1 by Tip60 leads to disruption of the DNMT1 and USP7 complex."

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"Importantly, both HDAC3 and USP7 decreased DNMT1 ubiquitination (XREF_FIG, DNMT1 IP)."

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"Consistent with previous studies that USP7 deubiquitinates and stabilizes DNMT1, knockdown of USP7 in several cell lines (HEK293T, HeLa, HCT116 p53-/- and p53 +/+ cells) resulted in a significant decrease in the DNMT1 protein level, but not in the DNMT1 messenger RNA level (XREF_FIG and XREF_SUPPLEMENTARY)."

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"Conversely, HDAC1 (histone deacetylase 1) induced DNMT1 deacetylation and HAUSP (herpes virus associated ubiquitin specific protease) modulated DNMT1 deubiquitination to stabilize DNMT1 44."

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"We recently showed that USP7 deubiquitinates DNMT1 and functions in concert with several other proteins to regulate DNMT1 stability."

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"Together, these observations suggest that multistep posttranslational modification events may be required to dissociate the UHRF1 and USP7 complex during M phase.Recent evidence has indicated that USP[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"FA decreased the ubiquitination of DNMT1 (p = 0.0753), DNMT3A (p = 0.0008) and DNMT3B (p < 0.0001) by decreasing UHRF1 (p < 0.0001) and USP7 (p < 0.0001)."

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"HAUSP deubiquitinates DNMT1 and protects it from proteasomal degradation."

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"USP7 inhibition increases ubiquitylation of DNMT1, and its degradation by the proteasome."

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"Both UHRF1 and DNMT1 are deubiquitinated and stabilized by USP7 [XREF_BIBR, XREF_BIBR], while UHRF1 is the negative regulator of DNMT1 [XREF_BIBR]."