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"On the other hand, ectopic expression of wild-type USP13, but not the C345A mutant which is still capable of interacting with PTEN (XREF_FIG), reduced the poly-ubiquitination of PTEN by 65% (XREF_FIG), suggesting that the enzymatic activity of USP13 is indispensable for USP13 dependent deubiquitination of PTEN."
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"On the other hand, ectopic expression of wild-type USP13, but not the C345A mutant which is still capable of interacting with PTEN (XREF_FIG), reduced the poly-ubiquitination of PTEN by 65% (XREF_FIG), suggesting that the enzymatic activity of USP13 is indispensable for USP13 dependent deubiquitination of PTEN."
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"In 2011, Yuan et al. found that USP13 could interact with the C-terminal domain of Beclin-1 subunit in the VPS34 complex and deubiquitinate Beclin-1, thereby enhancing the stability of the VPS34 complex, which would contribute to the formation of autophagosomes (Liu et al., 2011)."
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"Conversely, it was show that Beclin 1 is deubiquitinated by USP10 and USP13 and adding complexity, Beclin 1 itself controlled the protein stabilities of USP10 and USP13 by regulating their deubiquitinating activities, in turn regulating the levels of tumor suppressor p53 [XREF_BIBR]."
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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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"As USP13 functions as a deubiquitinase that also interacts with c-Myc (XREF_FIG) and the preferential expression of USP13 in GSCs positively regulates c-Myc protein levels (XREF_FIG), we hypothesized that USP13 might mediate deubiquitination of c-Myc protein to prevent its degradation and stabilize c-Myc in GSCs."
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"In ovarian tumors, upregulation of USP13 enhances deubiquitination and stabilization of ACLY (ATP citrate lyase) and OGDH (oxoglutarate dehydrogenase), two key enzymes that drive glutaminolysis, ATP generation, and lipid synthesis in cancer metabolism , and MCL1, a pivotal member of the antiapoptotic BCL-2 family of proteins ."
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"Taken together, these studies suggest that USP14 is involved in the occurrence and progression of multiple malignant tumors.Other USP family members: USP13, the main regulator of ovarian cancer energy metabolism, specifically deubiquitinates and stabilizes oxoglutarate dehydrogenase and ATP citrate lyase, which can catalyze fatty acid synthesis, glutaminolysis and mitochondrial respiration."
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"Taken together, these studies suggest that USP14 is involved in the occurrence and progression of multiple malignant tumors.Other USP family members: USP13, the main regulator of ovarian cancer energy metabolism, specifically deubiquitinates and stabilizes oxoglutarate dehydrogenase and ATP citrate lyase, which can catalyze fatty acid synthesis, glutaminolysis and mitochondrial respiration."
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"In ovarian tumors, upregulation of USP13 enhances deubiquitination and stabilization of ACLY (ATP citrate lyase) and OGDH (oxoglutarate dehydrogenase), two key enzymes that drive glutaminolysis, ATP generation, and lipid synthesis in cancer metabolism , and MCL1, a pivotal member of the antiapoptotic BCL-2 family of proteins ."
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"Further evidence showed that EMT might be the primary mechanism for the enhanced metastatic property in GC cells: USP13 and USP29 promoted TGF-β1-induced EMT through interacting with and deubiquitinating Snail, while USP3 facilitated this process by deubiquitinating SUZ12 (Wu et al. 2021; Zhang et al. 2022a, b; Qian et al. 2020)."
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"Protein interaction experiments demonstrated that USP13 could co-immunoprecipitate with endogenous TopBP1, and in vitro deubiquitination enzyme experiments showed that WT-USP13 could deubiquitinate TopBP1, while CA-USP13 could not, highlighting the requirement for USP13 ubiquitination activity (Kim et al., 2021)."
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"Interestingly, NEDD4-1 undergoes auto-ubiquitination that serves it as a scaffold for engaging the ubiquitin-specific protease 13 (USP13) to form a NEDD4-1/USP13 deubiquitination complex, which subsequently deubiquitinates and stabilizes VPS34 to induce phagophore nucleation in cancer cells."
USP13 affects Stomach Neoplasms
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USP13 deubiquitinates Stomach Neoplasms. 2 / 2
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USP13 deubiquitinates Stomach Neoplasms on D1. 1 / 1
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"Here, it was shown that USP13 negatively regulates Parkin ubiquitination, function, and solubility (Figure 5), negatively regulates the level, ubiquitination, and clearance of α-synuclein, and regulates proteasome activity independently of Parkin, which affects dopaminergic neuronal viability and motor performances in animal models."
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"To investigate whether USP13 mediated the deubiquitination of cohesin subunits, we cotransfected 293T cells with expression vectors for His ubiquitin and Myc-USP13, purified ubiquitinated proteins by Ni-NTA affinity chromatography, and performed Western blot with antibodies to SMC3 and RAD21 (XREF_FIG A)."
USP13 affects α-synuclein
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USP13 affects cell cycle protein
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USP13 deubiquitinates cell cycle protein on D1. 1 / 1
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USP13 affects TCRalpha
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"Although our results have not ruled out the possibility that USP13 may contribute to deubiquitination of TCRalpha with the assistance of a substrate recruiting adaptor in cells, the inability to deubiquitinate TCRalpha by purified USP13 suggests that the accumulation of ubiquitinated TCRalpha in USP13 knockdown cells is probably due to ERAD inhibition at a step downstream of ubiquitination, as shown in Bag6 depleted cells."
USP13 affects STING28
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"USP13 interacts with TAK1, inhibits TAK1 activation by removing ubiquitination of TAK1, and subsequently inhibits the NF-κB & MAPK signaling pathway activation (Fig. 9), thereby treating NAFLD as a latent molecular target.As a DUB enzyme, USP13 regulates the de-ubiquitination of multiple substrate proteins to participate in many cellular processes, including mitochondrial energy metabolism, DNA damage, autophagy, and endoplasmic reticulum-associated degradation [35]."