IndraLab

Statements

USP17L2 affects BRD4
1 | 9
USP17L2 deubiquitinates BRD4. 10 / 10
1 | 9
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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."
30057199
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"In a recent study, DUB3 was shown to promote BRD4 deubiquitination and stabilization in various cancer cell lines [XREF_BIBR]."
33327527
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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."
30057199
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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."
30057199
USP17L2 affects H2AX
1 | 1 3
USP17L2 deubiquitinates H2AX. 5 / 5
1 | 1 3
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"Dub3 controls DNA damage signalling by direct deubiquitination of H2AX"
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"Overexpression of DUB3 decreased monoubiquitination of γH2AX in the absence of an exogenous DNA damage source as well as post-IR [33]."
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"Moreover, Dub3 and H2AX interact and Dub3 deubiquitinates H2AX in vitro."
24704006
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"Moreover, Dub3 and H2AX interact and Dub3 deubiquitinates H2AX in vitro."
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"DUB3 (also known as USP17L2) directly interacts with and deubiquitylates H2AX [73]."
28764946
USP17L2 affects CDC25A
1 | 3
USP17L2 deubiquitinates CDC25A. 4 / 4
1 | 3
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"We also assessed the level of ubiquitin hydrolase DUB3 that is known to deubiquitylate and stabilize CDC25A 46."
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"DUB3 and USP17 mediates deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression [XREF_BIBR]."
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"Dub3 knockdown in cells increased Cdc25A ubiquitylation and degradation, resulting in reduced Cdk and Cyclin activity and arrest at G1/S and G2/M phases of the cell cycle."
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ubibrowser
No evidence text available
USP17L2 affects TWIST1
1 | 2
USP17L2 deubiquitinates TWIST1. 2 / 2
1 | 1
ubibrowser
"In this study, we identified Dub3 as a novel DUB for both Slug and Twist. We further found that Dub3 overexpression increased Slug and Twist protein levels in a dose-dependent manner, whereas Dub3-knockdown decreased their protein levels."
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"Dub3 deubiquitinates Slug and Twist."
29088851
Modified USP17L2 leads to the deubiquitination of TWIST1. 1 / 1
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"Co-expression of wild-type (WT) Dub3 almost completely abolished ubiquitination of Slug and Twist, while co-expression of CS-Dub3 did not show this effect (lane 2 vs lane 3 in both upper panels, Figure XREF_FIG)."
29088851
USP17L2 affects SNAIL1
| 3
USP17L2 deubiquitinates SNAIL1. 3 / 3
| 3
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"In addition, WT DUB3, but not the C89S mutant, markedly decreased SNAIL1 ubiquitination in vitro (XREF_FIG)."
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"DUB3 deubiquitinates and stabilizes SNAIL1."
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"Since DUB3 deubiquitinates and stabilizes SNAIL1 and consequently decreases E-cadherin expression, we hypothesized that DUB3 is critical for breast cancer cell migration and invasion in vitro."
28067227
USP17L2 affects SNAI2
1 | 2
USP17L2 deubiquitinates SNAI2. 2 / 2
1 | 1
ubibrowser
"In this study, we identified Dub3 as a novel DUB for both Slug and Twist. We further found that Dub3 overexpression increased Slug and Twist protein levels in a dose-dependent manner, whereas Dub3-knockdown decreased their protein levels."
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"Dub3 deubiquitinates Slug and Twist."
29088851
Modified USP17L2 leads to the deubiquitination of SNAI2. 1 / 1
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"Co-expression of wild-type (WT) Dub3 almost completely abolished ubiquitination of Slug and Twist, while co-expression of CS-Dub3 did not show this effect (lane 2 vs lane 3 in both upper panels, Figure XREF_FIG)."
29088851
USP17L2 affects SUDS3
1 | 1
USP17L2 deubiquitinates SUDS3. 2 / 2
1 | 1
ubibrowser
"We previously reported that the USP17 deubiquitinating enzyme having hyaluronan binding motifs (HABMs) interacts with human SDS3 (suppressor of defective silencing 3) and specifically deubiquitinates Lys-63 branched polyubiquitination of SDS3 resulting in negative regulation of histone deacetylase (HDAC) activity in cancer cells."
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"DUB-3 (also known as USP17) is a cytokine-inducible human DUB that was found to deubiquitinate SDS3 and block proliferation in HeLa cells [93]."
31208841
USP17L2 affects LATS2
| 2
USP17L2 deubiquitinates LATS2. 1 / 1
| 1
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"Interestingly DUB3 also interacts with and deubiquitinates AMOT, AMOTL1, and the kinases LATS1 and LATS2 to promote their stability and in so doing decrease YAP activity [124]."
28923280
Modified USP17L2 leads to the deubiquitination of LATS2. 1 / 1
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"LATS2 ubiquitylation was markedly suppressed by overexpression of DUB3, but not by the catalytically inactive C89S form of DUB3 (XREF_SUPPLEMENTARY)."
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USP17L2 affects ITCH
| 2
Modified USP17L2 leads to the deubiquitination of ITCH. 1 / 1
| 1
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"Expression of DUB3 strongly reduced the amount of poly-ubiquitylated ITCH (XREF_FIG)."
28061504
USP17L2 deubiquitinates ITCH. 1 / 1
| 1
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"First, DUB3 deubiquitinates and stabilizes the E3 ligase ITCH."
28923280
USP17L2 affects AMOT
| 2
USP17L2 deubiquitinates AMOT. 1 / 1
| 1
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"Interestingly DUB3 also interacts with and deubiquitinates AMOT, AMOTL1, and the kinases LATS1 and LATS2 to promote their stability and in so doing decrease YAP activity [124]."
28923280
Modified USP17L2 leads to the deubiquitination of AMOT. 1 / 1
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"Reciprocally, overexpression of DUB3 reduced the ubiquitylation of AMOT, while the inactive C89S DUB3 mutant had no effect (XREF_SUPPLEMENTARY)."
28061504
USP17L2 affects Snail1
| 1
Modified USP17L2 leads to the deubiquitination of Snail1. 1 / 1
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"However, co-expression of WT-Dub3 almost completely abolished Snail1 ubiquitination while the CS-Dub3 did not have this effect (lanes 2 versus 3, XREF_FIG)."
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USP17L2 affects SNAI1
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USP17L2 deubiquitinates SNAI1. 1 / 1
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ubibrowser
"CDK4/6-mediated activation of DUB3 is essential to deubiquitinate and stabilize SNAIL1"
28067227
USP17L2 affects SIRT7
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USP17L2 deubiquitinates SIRT7. 1 / 1
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"We find that the deubiquitinase USP17L2 interacts with and deubiquitinates SIRT7, thereby increasing SIRT7 protein stability."
36040642
USP17L2 affects RCE1
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USP17L2 deubiquitinates RCE1. 1 / 1
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ubibrowser
"we show that this effect is caused by the loss of RCE1 catalytic activity as a result of its deubiquitination by USP17."
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USP17L2 affects RAS
| 1
USP17L2 deubiquitinates RAS. 1 / 1
| 1
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"DUB-3 also influenced the Ras/MEK/ERK signaling pathway and deubiquitinated Ras converting enzyme 1 (RCE1), decreasing proliferation of cells [XREF_BIBR]."
31208841
USP17L2 affects NFE2L2
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USP17L2 deubiquitinates NFE2L2. 1 / 1
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"DUB3 deubiquitinates and stabilizes NRF2 in chemotherapy resistance of colorectal cancer."
30778200
USP17L2 affects LGMN
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USP17L2 deubiquitinates LGMN. 1 / 1
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ubibrowser
"We demonstrate that TRAF6 ubiquitinates the proform of AEP through K63-linked polyubiquitin, reversible by USP17, and forms a complex with HSP90伪 to subsequently promote pro-AEP intracellular stability as well as secretion.?"
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USP17L2 affects LATS1
| 1
USP17L2 deubiquitinates LATS1. 1 / 1
| 1
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"Interestingly DUB3 also interacts with and deubiquitinates AMOT, AMOTL1, and the kinases LATS1 and LATS2 to promote their stability and in so doing decrease YAP activity [124]."
28923280
USP17L2 affects KLF4
| 1
USP17L2 deubiquitinates KLF4. 1 / 1
| 1
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"The results showed that DUB3 upregulated KLF4 expression by deubiquitinating and stabilizing KLF4 protein in HCC cells through binding with KLF4."
35383144
USP17L2 affects IFIH1
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USP17L2 deubiquitinates IFIH1. 1 / 1
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ubibrowser
"Taken together, our findings suggest that USP17 functions through deubiquitination of RIG-I and MDA5 to regulate virus-induced type I IFN signaling."
20368735
USP17L2 affects HAS2
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USP17L2 deubiquitinates HAS2. 1 / 1
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ubibrowser
"?Several DUBs were found to decrease the ubiquitination of 6myc-HAS2, among which, the most effective were USP17 and USP4. USP17 efficiently removed polyubiquitination, whereas USP4 preferentially removed monoubiquitination of 6myc-HAS2."
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USP17L2 affects FAM126A
| 1
USP17L2 leads to the deubiquitination of FAM126A. 1 / 1
| 1
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"The results showed that DUB3 upregulated KLF4 expression by deubiquitinating and stabilizing KLF4 protein in HCC cells through binding with KLF4."
35383144
USP17L2 affects DELEC1
| 1
USP17L2 deubiquitinates DELEC1. 1 / 1
| 1
trips
"USP17 binds and deubiquitylates DEC1, markedly extending its half-life."
25202122
USP17L2 affects DDX58
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USP17L2 deubiquitinates DDX58. 1 / 1
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ubibrowser
"Taken together, our findings suggest that USP17 functions through deubiquitination of RIG-I and MDA5 to regulate virus-induced type I IFN signaling."
20368735
USP17L2 affects AMOTL1
| 1
USP17L2 deubiquitinates AMOTL1. 1 / 1
| 1
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"Interestingly DUB3 also interacts with and deubiquitinates AMOT, AMOTL1, and the kinases LATS1 and LATS2 to promote their stability and in so doing decrease YAP activity [124]."
28923280