IndraLab

Statements

USP37 deubiquitinates MCM7. 12 / 12
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"Although USP37 depletion enhanced this residual ubiquitylation of MCM7 (Fig. 4c, lane 5), most MCM7 remained unmodified, and importantly, the residual ubiquitylation was not dependent on TRAIP (Fig. 4c, lane 6)."
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"Proteomics and enzyme assays revealed USP37 interacts with the CMG complex to deubiquitinate MCM7, thus antagonizing replisome disassembly."
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"USP37 regulates the CMG complex by deubiquitinating MCM7."
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"To test if USP37 can deubiquitinate MCM7 in vitro, we mixed recombinant USP37 with our ubiquitinated protein eluate and assessed MCM7 deubiquitination over time by MCM7 immunoblotting."
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"This was dependent on USP37 activity, since USP37 harboring a C-S mutation of its active site cysteine at position 350 was unable to promote MCM7 deubiquitination (Fig. 4D compare lanes 7 and 8)."
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"Thus, USP37 can deubiquitinate MCM7, establishing that MCM7 ubiquitination is directly antagonized by USP37."
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"Collectively, these experiments demonstrate that USP37 can deubiquitinate MCM7 and suggest that it does so by preferentially removing long ubiquitin polymers."
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"Interestingly, in our hands, USP37 reduced but did not completely abolish ubiquitination of MCM7, suggesting that it may be removing a specific chain or chain type(s), rather than deubiquitinating the proximal ubiquitin conjugated directly onto MCM7 (Fig. 4D)."
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"Here, we demonstrate that premature CMG unloading is prevented by the USP37 deubiquitinase, which antagonizes MCM7 ubiquitination, thereby limiting aberrant unloading of the CMG helicase."
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"We show here that MCM7 ubiquitination is antagonized by USP37."
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"In the presence of the p97 inhibitor NMS-873 (p97-i), USP37 depletion led to polyubiquitylation of MCM7 and MCM6 on chromatin, which was most evident from loss of the unmodified forms of these proteins (Fig. 3b, lane 10 vs. 12)."
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"In vitro deubiquitination of Ub-MCM7 by recombinant USP37."
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