IndraLab

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USP1 deubiquitinates MYC. 7 / 7
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"USP1 Deubiquitinates and Stabilizes c-MYC."

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"Our study showed that inhibition of USP1 by shRNA or pimozide treatment significantly increased the ubiquitination of MAX/MYC and reduced the protein levels of MAX/MYC in rituximab/chemotherapy resistant DLBCL cells, which led to the decrease of MYC target genes and the growth inhibition of lymphoma cells in the cell or patient-derived DLBCL mouse model."

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"In summary, these results suggested that USP1 deubiquitinates and stabilizes c-MYC."

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"Finally, we investigated whether USP1 could inhibit the ubiquitination of c-MYC and found that USP1, but not USP1 C90S, decreased the ubiquitination level of c-MYC, thus increasing its stability (Figure 5H)."

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"USP1 is an oncogene that deubiquitinates and stabilizes c-MYC, thereby promoting cancer progression in vitro and in vivo."

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"Together, these data demonstrated that USP1 deubiquitinated and stabilized MAX and MYC proteins in rituximab/chemotherapy resistant DLBCL cells."

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"Overexpression of USP1 prolonged the half-life of MAX/MYC protein and decreased the ubiquitination of MAX/MYC protein."