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USP13 deubiquitinates BECN1. 9 / 9
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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."

"While A20 inhibits PtdIns3P signaling by removing the TRAF6-dependent Lys63-linked chains from Beclin 1, the enzymes USP10 and USP13 prevent PI3K-III complex components from their degradation and, therefore, support autophagy. Interestingly enough, USP10 also stabilizes p53, which, in turn, triggers the degradation of Beclin 1 and VPS34 in order to prevent autophagy."

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

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

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

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

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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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"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."