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USP17L2 deubiquitinates BRD4. 10 / 10
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"Based on these genomic data and our finding that NCOR2 represses DUB3 expression in cultured cells, we hypothesized that loss of NCOR due to deletions or mutations results in DUB3 upregulation, which [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Knockdown of DUB3 completely abolished NCOR2-depletion-induced elevation of BRD4 protein and BRD4 protein polyubiquitination but had no effect on BRD4 mRNA expression."
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"In a recent study, DUB3 was shown to promote BRD4 deubiquitination and stabilization in various cancer cell lines [XREF_BIBR]."
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"Furthermore, PD0332991 treatment also increased BRD4 polyubiquitination, shortened the BRD4 protein half-life, and reversed DUB3 mediated deubiquitination of BRD4 in DU145 cells."
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"In support of these findings, we show that inhibition of BRD4 by JQ1 blocks NCOR2 mRNA expression, which in turn dismisses NCOR2 mediated repression of DUB3 and DUB3 mediated deubiquitination of BRD4."
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"In agreement with these findings, knockdown of DUB3 shortened the BRD4 protein half-life and dramatically increased endogenous BRD4 ubiquitination in PC-3 cells."
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"DUB3 promotes BET inhibitor resistance and cancer progression by deubiquitinating BRD4."
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"DUB3 Deubiquitinates BRD4 to Promote Prostate Cancer Progression."
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"For example, BRD4 interacted with and was de-ubiquitinated by deubiquitinase DUB3."
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"Here, we demonstrate that the deubiquitinase DUB3 binds to BRD4 and promotes its deubiquitination and stabilization."
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