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USP13 deubiquitinates MYC. 7 / 9
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"In cholangiocarcinoma, TGF-β signaling triggers the phosphorylation of CLK3, a serine/threonine kinase that directly phosphorylates USP13 at Y708 and facilitates USP13 interaction with c-Myc (Zhou et al., 2020); in GSCs, USP13 can enhance the stability through deubiquitinating c-Myc, activating purine synthesis mediated by c-Myc and inducing the tumorigenesis of GSCs (Fang et al., 2017); in hepatocellular carcinoma, knockdown of USP13 by shRNA can markedly downregulate c-Myc expression, resisting xenograft tumor growth of HCC (Huang et al., 2020)."

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"The ubiquitination assay demonstrated that disruption of USP13 by shRNA markedly increased c-Myc ubiquitination and reduced c-Myc protein level in GSCs (XREF_FIG)."

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"Furthermore, USP13 can deubiquitinate and stabilise ACLY and OGDH and c-Myc in ovarian cancer and glioblastoma, respectively, thereby functioning as an oncogene [XREF_BIBR, XREF_BIBR]."

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"Our data have demonstrated that USP13 mediates deubiquitination of c-Myc, whereas FBXL14 facilitates c-Myc ubiquitination in glioma cells."

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"It has been reported that c-Myc can be de-ubiquitinated by USP13 [33]."

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"Moreover, USP13 knockdown increased c-Myc ubiquitination, whereas FBXL14 knockdown reduced c-Myc ubiquitination (XREF_FIG)."

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"In these tumors, USP13 deubiquitinates and stabilizes some oncogenes, including MCL1 [19, 20], Myc [8], MITF [21] and ZHX2 [22]."