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USP13 deubiquitinates BECN1. 11 / 13
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"Likewise, USP13, which deubiquitinates BECN1 and stabilizes PIK3C3 complexes, is amplified in LUSQ."

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"Furthermore, the presence of spautin-1 inhibited the deubiquitination of Beclin1 mediated by USP10 and USP13."

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"It promotes the degradation of Vps34 complexes by inhibiting USP10 and USP13, two ubiquitin specific peptidases that target the deubiquitination of Beclin-1."

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"In addition, USP10 or USP13 can deubiquitinate and stabilize Beclin 1 in promoting autophagy ."

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"Specific and potent autophagy inhibitor-1 (Spautin-1) was identified to inhibit USP10 and USP13, which deubiquitinate the Beclin 1 subunit of Vsp34 complex, and thus promoted the degradation of Vsp34 PI3 kinase complex."

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"We demonstrate that USP10 and USP13 can both mediate the deubiquitination of Beclin1."

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"Recent studies indicated that USP13 can deubiquitinate and regulate protein levels of Beclin-1, microphathalmia associated transcription factor, Siah2, phosphatase and tensin homolog, and STAT-1, and the deubiquitination process of USP13 could also be orchestrated by Beclin-1."

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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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"At the molecular level, the authors convincingly demonstrate that USP13 directly interacts with and deubiquitinates Beclin-1 (Figure 1B)."

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"USP10 and USP13 have been shown to mediate the deubiquitination of Beclin 1, thereby stabilizing the Vps34 complex XREF_BIBR."