IndraLab

Statements

USP28 activates STAT3. 13 / 13
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"Moreover, the CHX chase assay revealed that overexpression of USP28 prolonged the half-life of STAT3 protein in NSCLC cells, which further suggested that USP28 stabilized STAT3 protein (XREF_FIG)."
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"USP28 increases the stability of STAT3."
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"These results demonstrated that USP28 was functional in NSCLC cells, and promoted NSCLC cell growth by inducing STAT3 signaling."
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"As shown in XREF_FIG, overexpression of USP28 upregulated STAT3 protein in a dose dependent manner, but the mRNA level of STAT3 was not changed obviously (XREF_FIG)."
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"In addition, the immunoblotting assay also revealed that overexpression of USP28 enhanced the STAT3 signaling in NSCLC cells (XREF_FIG)."
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"USP28 is highly expressed and mediates STAT3 signaling by stabilizing STAT3 in NSCLC cells, which suggests that USP28 can be a potential target for NSCLC therapy in the future."
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"Herein, we identified that USP28, a deubiquitinase aberrantly upregulated in patients with ADPKD, selectively removed K48-linked polyubiquitination and reversed protein degradation of signal transducer and activator of transcription 3 (STAT3)."
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"As shown in XREF_FIG, overexpression of USP28 significantly upregulated STAT3 derived luciferase activity, but another USP isoform, USP25, had no effect on STAT3 luciferase activity."
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"USP28 mediates STAT3 signaling in NSCLC cells."
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"As stated before, USP28 mediated STAT3 signaling by stabilizing STAT3 protein, which suggested that USP28 was functional in NSCLC cells."
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"In this study, the deubiquitinating enzyme USP28 was found to mediate STAT3 signaling in NSCLC cells."
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"XREF_BIBR In this study, we found that USP28 mediated STAT3 signaling and promoted NSCLC cell growth (XREF_FIG and XREF_FIG)."
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"We found that USP28 mediated STAT3 signaling in NSCLC cells."
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