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USP20 binds HERC2. 32 / 32
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"As shown in Figure XREF_FIG, the interaction between HERC2 and USP20 decreased at early time point following DNA damage and then increased at later time point."
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"In unstressed cells, HERC2 binds USP20 to maintain a low basal level of USP20 in cells."
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"Co-immunoprecipitation assays revealed that both HERC2 and CLASPIN were present in the USP20 immunocomplex and both USP20 and CLASPIN were in the HERC2 immunocomplex, suggesting that HERC2, USP20 and CLASPIN form a complex."
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"We found that treating cells with the pan PIKK inhibitor caffeine blocked the disassociation of USP20 and HERC2 after UV treatment (Figure xref ), suggesting that PIKKs might be involved in the regulation of USP20-HERC2 interaction."
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"We found that the presence of USP20 in the HERC2 immunocomplex decreased upon HU treatment, so did the presence of HERC2 in the FALG-USP20 immunocomplex, whereas the interaction between USP20 (4SA) and HERC2 did not decrease in response to HU treatment."
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"We next studied how HERC2-USP20 interaction is regulated by the DDR pathway."
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"We confirmed the interaction between USP20 and HERC2 by endogenous Co-IP."
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"One is that USP20 phosphorylation itself affects the binding between USP20 and HERC2."
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"On the other hand, USP20 is phosphorylated by ATR, which disrupts the interaction between USP20 and HERC2, resulting in USP20 stabilization."
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"Mechanistically, the phosphorylation of USP20 by ATR disrupts the interaction between HERC2 and USP20 and is responsible for USP20 upregulation following the DDR."
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"We found that the presence of USP20 in the HERC2 immunocomplex decreased upon HU treatment (Figure xref ), so did the presence of HERC2 in the FALG-USP20 immunocomplex, whereas the interaction between USP20(4SA) and HERC2 did not decrease in response to HU treatment (Figure xref )."
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"As shown in Figure xref , the interaction between HERC2 and USP20 decreased at early time point following DNA damage and then increased at later time point."
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"HERC2 interacts with USP20, a DUB that is recruited to DSBs and is involved in checkpoint signalling in response to replication stress and HR repair [ xref – xref ]."
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"Further mapping of the USP20-HERC2 interaction showed that the enzymatic domain of USP20, is required for the interaction between USP20 and HERC2."
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"We confirmed the interaction between USP20 and HERC2 by endogenous Co-IP (Figure xref and xref )."
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"During cell recovery from genotoxic stress, USP20 binds to HERC2 again and gets degraded."
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"During cell recovery from genotoxic stress, USP20 binds to HERC2 again and gets degraded."
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"Consistent with this, we found that HERC2 binds the catalytic domain (aa 145–686) of USP20, which includes all four phosphorylation sites."
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"On the other hand, USP20 is phosphorylated by ATR, which disrupts the interaction between USP20 and HERC2, resulting in USP20 stabilization."
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"As USP20 ubiquitination decreases following replication stress, we next studied whether the USP20-HERC2 interaction is subjected to regulation by the DDR pathway."
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"Further mapping of the USP20-HERC2 interaction showed that the enzymatic domain of USP20, is required for the interaction between USP20 and HERC2 (Supplementary Figure S3A)."
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"Consistent with this, we found that HERC2 binds the catalytic domain (aa 145-686) of USP20, which includes all four phosphorylation sites."
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"In unstressed cells, HERC2 binds USP20 to maintain a low basal level of USP20 in cells."
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No evidence text available
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"Mechanistically, the phosphorylation of USP20 by ATR disrupts the interaction between HERC2 and USP20 and is responsible for USP20 upregulation following the DDR."
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"Chk1 activation is indirectly regulated via modulation of Claspin stability by ubiquitination and deubiquitination events, involving the HERC2 and USP20 complex [49,50]."
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