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USP10 deubiquitinates PTEN. 9 / 10
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"Additionally, we found that USP10 stabilized PTEN protein in a dose dependent manner, and inhibited Lys-48-linked polyubiquitylation of PTEN."

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"However, USP10 can interact with PTEN to reduce K63-linked ubiquitination of PTEN mediated by the E3 ligase TRIM25, restore PTEN activity and reduce PIP3 production, thereby inhibiting the signal transduction of mammalian target of rapamycin (mTOR) in NSCLC cells (71)."

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"Furthermore, several DUBs, including HAUSP/USP7, USP10, USP11, USP13, OTUD3, and Ataxin-3 have been shown to reverse the ubiquitination of PTEN, a key antagonist in the PI3K growth-promoting pathway, implicating its function in cancer-specific contexts [15]."

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"Furthermore, USP10 can also interact with and deubiquitinate PTEN, USP10 inhibition stimulates tumor growth and invasion, but this effect can be abolished by reinserting PTEN (Sun et al., 2018)."

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"In this study, we identified that USP10 can deubiquitinate PTEN and AMPKalpha and the stabilization of these two proteins will subsequently suppress the activation of AKT and mTOR in HCC cells."

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"In addition, in line with our study, two different groups have also reported that USP10 deubiquitinates and stabilizes PTEN and AMPKalpha in lung cancer and colon cancer cells [16, 27]."

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"In line with our hypothesis, USP10 decreased PTEN polyubiquitination in a concentration-dependent manner as evidenced by overexpression (Fig. 1D) or siRNA knockdown (Fig. 1E)."

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"These results further demonstrated that USP10 antagonizes TRIM25 in PTEN ubiquitination modification without affecting its stability."

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"51 In contrast, Lu et al. indicated that USP10 suppresses hepatocellular tumor progression by interacting with and deubiquitinating PTEN and AMPKa."