IndraLab

Statements

ECT2 activates USP7. 7 / 7
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"ECT2 promotes USP7 intermolecular self-association , - deubiquitination and - stabilization Since ECT2 could not allosterically activate USP7 and it possesses neither E3 ligase nor deubiquitinase activity , we hypothesized that ECT2-promoted USP7 stabilization is likely through enhancing the association of USP7 with other deubiquitinase ( s ) or protecting it from ubiquitination by E3 ligase ( s ) ."
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"These results indicated that USP7 targets ECT2 for deubiquitination, indicating that ECT2 is a bona fide substrate of USP7."
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"Since ECT2 could not allosterically activate USP7 and it possesses neither E3 ligase nor deubiquitinase activity, we hypothesized that ECT2 promoted USP7 stabilization is likely through enhancing the association of USP7 with other deubiquitinase (s) or protecting it from ubiquitination by E3 ligase (s)."
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"Considering that the association of USP7 with ECT2 also requires the UBL domain, we wondered whether ECT2 could allosterically enhance the deubiquitinase activity of USP7."
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"Although ECT2 fails to activate the enzymatic activity of USP7, we surprisingly found that ECT2 depletion resulted in markedly downregulation of several USP7 substrates including PHF8 XREF_BIBR, RNF168 XREF_BIBR, and MDM2 XREF_BIBR at protein, but not mRNA level."
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"However, overexpression of ECT2 in USP7 depleted cells, in which the protein level of overexpressed ECT2 was higher than the endogenous one in control cells, failed to rescue USP7 deficiency associated effects."
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"Since ECT2 could not allosterically activate USP7 and it possesses neither E3 ligase nor deubiquitinase activity, we hypothesized that ECT2-promoted USP7 stabilization is likely through enhancing the association of USP7 with other deubiquitinase(s) or protecting it from ubiquitination by E3 ligase(s)."
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