IndraLab

Statements


USP2 affects Cyclin
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USP2 deubiquitinates Cyclin on D1. 5 / 5
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"reported that USP2 specifically deubiquitinates and stabilizes cyclin D1, whereas knockdown of this protease causes cyclin D1 degradation and growth arrest in cancer cells dependent on this cell cycle regulator."

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"In particular, it has been recently shown that USP-2 deubiquitinates cyclin D1, prevents degradation, accumulates cyclin D1 and finally leads to cell cycle progression from G1 to S phase (Lee et al., [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Cyclin D1 ubiquitination is reversed by the deubiquitinases USP2 and USP22."

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"Several compounds have been shown to suppress the activity of USP2, which can promote the deubiquitylation and stability of cyclin D1 [137]."

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"In a screen of potential deubiquitination enzymes, Shan et al. identified USP2 to specifically deubiquitinate cyclin D1, preventing the degradation of cyclin D1, and leading to the accumulation of cyclin D1."
USP2 affects PER1
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USP2 deubiquitinates PER1. 4 / 4
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"In light of the shorter half-life of USP2 (compared to that of PER1) (XREF_FIG) and of its rhythmic expression peaking almost simultaneously with that of PER1, the deubiquitination of PER1 by USP2 could be restricted to a specific circadian time and therefore be altering the function and/or localization of PER1 to fine tune the molecular clock in physiological conditions."

"Recently, we showed that the deubiquitinating enzyme ubiquitin-specific peptidase 2 (USP2) associates with clock proteins and deubiquitinates PERIOD1 (PER1) but does not affect its overall stability."

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"Deubiquitination of PER1 by USP2 does not stabilize it."

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"USP2 is essential to deubiquitinating PER1, CRY1 and CRY2 in vivo [54–57]."
USP2 affects MDM2
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USP2 deubiquitinates MDM2. 4 / 4
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"USP2 deubiquitinates both MDM2 and MDMX [XREF_BIBR, XREF_BIBR] whereas USP4 deubiquitinates ARF-BP1 [XREF_BIBR], another ubiquitin ligase for p53, thus indirectly destabilizing p53 and inhibiting its function."

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"Specifically, protein-protein interaction assays using the bacterial two-hybrid system showed that USP2 can deubiquitinate MDM2 and promotes p53 degradation, showing the association between USP2 and MDM2 (Stevenson et al., 2007)."

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"USP2 deubiquitinates and stabilizes MDM2 thus inhibiting the proapoptotic activity of p53."
USP2 affects LDLR
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USP2 deubiquitinates LDLR. 4 / 4
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"The authors attempt to answer this question by introducing a tripartite complex model, in which USP2 interacts with LDLR at the plasma membrane in an IDOL dependent manner to deubiquitylate and stabilize both LDLR and IDOL."

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"Such a temporal expression pattern would leave little opportunity to alleviate the USP2 mediated antagonism of IDOL, and the tripartite complex model would imply that IDOL is constantly engaged in a futile reaction, in which its ubiquitylation of LDLR is immediately reversed by USP2."

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"We identify a tri and partite complex encompassing IDOL, USP2, and LDLR and demonstrate that in this context USP2 promotes deubiquitylation of the LDLR and prevents its degradation."

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"In summary, USP2 activity leads to the deubiquitylation and stabilization of cell surface LDLR in and IDOL dependent manner, but it remains uncertain exactly why such a phenomenon is accompanied by an extended IDOL protein half-life."
USP2 affects TWIST1
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USP2 deubiquitinates TWIST1. 2 / 2
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"Furthermore, TJP1 recruited USP2, which deubiquitinated TWIST1, thereby protecting TWIST1 from proteasome-mediated protein degradation."

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"USP2 regulates Bmi1 and EMT by Twist stabilization and prevents Twist ubiquitination driven by beta-TrCP and subsequent proteasome mediated protein degradation."
Modified USP2 leads to the deubiquitination of TWIST1. 1 / 1
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"Our data showed that beta-TrCP-driven Twist ubiquitination is abolished by overexpression of USP2."
USP2 affects MYLIP
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USP2 deubiquitinates MYLIP. 2 / 2
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"In summary, USP2 activity leads to the deubiquitylation and stabilization of cell surface LDLR in and IDOL dependent manner, but it remains uncertain exactly why such a phenomenon is accompanied by an extended IDOL protein half-life."

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"The authors attempt to answer this question by introducing a tripartite complex model, in which USP2 interacts with LDLR at the plasma membrane in an IDOL dependent manner to deubiquitylate and stabilize both LDLR and IDOL."
Modified USP2 leads to the deubiquitination of MYLIP. 1 / 1
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"USP2 overexpression was shown to decrease IDOL ubiquitylation, but it remains unknown which type of ubiquitin linkages on IDOL are edited by USP2."
USP2 affects MDM4
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USP2 deubiquitinates MDM4. 3 / 3
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"USP2 deubiquitinates both Mdm2 and MdmX."

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"MdmX, another target of Mdm2, is also deubiquitinated by USP2."

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"USP2 deubiquitinates both MDM2 and MDMX [XREF_BIBR, XREF_BIBR] whereas USP4 deubiquitinates ARF-BP1 [XREF_BIBR], another ubiquitin ligase for p53, thus indirectly destabilizing p53 and inhibiting its function."
USP2 affects CRY1
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USP2 deubiquitinates CRY1. 3 / 3
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"In addition to PER1 and BMAL1, USP2 deubiquitinates CRY1 in cultured cells in response to a serum shock, and in the mouse liver, Usp2 knockdown increases CRY ubiquitination and decreases CRY1 protein levels."

"USP2a protein deubiquitinates and stabilizes the circadian protein CRY1 in response to inflammatory signals."

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"USP2 is essential to deubiquitinating PER1, CRY1 and CRY2 in vivo [54–57]."
USP2 affects RIPK1
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USP2 deubiquitinates RIPK1 on K377. 1 / 1
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No evidence text available
USP2 deubiquitinates RIPK1. 1 / 1
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"?We have found that the ubiquitin-specific protease USP2a has a pivotal role in the decision for cell death or survival by the TNFR1 complex. This enzyme is a novel component of the TNFR1 complex that is recruited upon ligand binding and controls the signalling activity of the TNFR1-interacting protein RIP1 by removing its K63-linked ubiquitin chains.?"
USP2 affects MMP2
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USP2 leads to the deubiquitination of MMP2. 2 / 2
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"It has been proven that USP2 promotes breast cancer metastasis by deubiquitinating MMP2 XREF_BIBR."
USP2 affects Imd
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USP2 deubiquitinates Imd. 2 / 2
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"USP2, for instance, deubiquitinates Imd, promoting its degradation."

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"Identifying USPs regulating immune signals in Drosophila : USP2 deubiquitinates Imd and promotes its degradation by interacting with the proteasome."
USP2 affects antithrombin
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USP2 deubiquitinates antithrombin. 1 / 1
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"3.5 | USP2 deubiquitinates and stabilizes antithrombin."
USP2 affects TRAF2
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USP2 deubiquitinates TRAF2. 1 / 1
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"USP2a similarly de-ubiquitinates TRAF2, a ubiquitin-ligase recruited to the TNFR1 complex.?"
USP2 affects TP53
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USP2 deubiquitinates TP53. 1 / 1
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"Unlike USP7, USP2 does not deubiquitinate p53 (9)."
USP2 affects SMAD7
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USP2 leads to the deubiquitination of SMAD7. 1 / 1
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"Specifically, USP2 interacted with SMAD7 and prevented SMAD7 ubiquitination."
USP2 affects SLC22A1
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USP2 deubiquitinates SLC22A1. 1 / 1
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"We also suggest that the deubiquitination of Oct-1 transcription factors by USP2 is involved in the transcriptional regulation of cytokine genes."
USP2 affects SKP2
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USP2 deubiquitinates SKP2. 1 / 1
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"We first screened a panel of DUBs and found that both USP2 and USP21 bound to endogenous SKP2, but only USP2 deubiquitylated and stabilized SKP2 protein."
USP2 affects SIRT1
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USP2 deubiquitinates SIRT1. 1 / 1
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USP2 affects SCNN1G
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USP2 deubiquitinates SCNN1G. 1 / 1
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"The surface expression of ENaC components is directed by the ubiquitination of ENaC by NEDD4L, an ENaC-specific E3 ubiquitin ligase, and is regulated by the deubiquitination of ENaC by USP2.?"
USP2 affects SCNN1B
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USP2 deubiquitinates SCNN1B. 1 / 1
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"The surface expression of ENaC components is directed by the ubiquitination of ENaC by NEDD4L, an ENaC-specific E3 ubiquitin ligase, and is regulated by the deubiquitination of ENaC by USP2.?"
USP2 affects SCNN1A
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USP2 deubiquitinates SCNN1A. 1 / 1
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"Fine-tuning of renal sodium reabsorption and excretion depends on the epithelial sodium channel protein (ENaC: protein complex of SCNN1A, SCNN1B, and SCNN1G). The surface expression of ENaC components is directed by the ubiquitination of ENaC by NEDD4L, an ENaC-specific E3 ubiquitin ligase, and is regulated by the deubiquitination of ENaC by USP2."
USP2 affects PTH1R
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USP2 deubiquitinates PTH1R. 1 / 1
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"Usp2 is a deubiquitination enzyme targeting various factors including CyclinD1 in cancer cells and PTH receptor 1 in osteoblasts."
USP2 affects PERIOD1
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USP2 deubiquitinates PERIOD1. 1 / 1
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"Recently, we showed that the deubiquitinating enzyme ubiquitin specific peptidase 2 (USP2) associates with clock proteins and deubiquitinates PERIOD1 (PER1) but does not affect its overall stability."
USP2 affects IL32
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USP2 deubiquitinates IL32. 1 / 1
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"USP2 deubiquitinated and stabilized tAIF, thus promoting AIF mediated cell death."
USP2 affects GRIA
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USP2 leads to the deubiquitination of GRIA. 1 / 1
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"Given the same type of deubiquitinating enzyme (USP46) is able to deubiquitinate AMPA receptors, and knockdown of USP46 elevated AMPA receptor ubiquitination and reduced AMPA receptor expression in hi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP2 affects FASN
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USP2 deubiquitinates FASN. 1 / 1
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"Here we show that the isopeptidase USP2a (ubiquitin-specific protease-2a) interacts with and stabilizes fatty acid synthase (FAS),?"
USP2 affects FAS
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USP2 deubiquitinates FAS. 1 / 1
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"USP2a can also deubiquitinate Fas preventing apoptosis in PCa"
USP2 affects ENaC
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Modified USP2 leads to the deubiquitination of ENaC. 1 / 1
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"Likewise, overexpression of USP2 causes decreased ubiquitination of ENaC and increases its activity at the plasma membrane."
USP2 affects ELOVL6
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USP2 deubiquitinates ELOVL6. 1 / 1
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"In various cancers, including prostate cancer and ovarian carcinoma, upregulation of USP2 leads to an increase in the levels of deubiquitinated substrates such as fatty acid synthase, MDM2, cyclin D1 and Aurora-A."
USP2 affects CRYL1
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USP2 leads to the deubiquitination of CRYL1. 1 / 1
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"In addition to PER1 and BMAL1, USP2 deubiquitinates CRY1 in cultured cells in response to a serum shock, and in the mouse liver, Usp2 knockdown increases CRY ubiquitination and decreases CRY1 protein levels."
USP2 affects CRY2
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USP2 deubiquitinates CRY2. 1 / 1
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"USP2 is essential to deubiquitinating PER1, CRY1 and CRY2 in vivo [54–57]."
USP2 affects CCND1
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USP2 deubiquitinates CCND1. 1 / 1
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"Usp2 is a deubiquitination enzyme targeting various factors including CyclinD1 in cancer cells and PTH receptor 1 in osteoblasts."
USP2 affects AURKA
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USP2 deubiquitinates AURKA. 1 / 1
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"In various cancers, including prostate cancer and ovarian carcinoma, upregulation of USP2 leads to an increase in the levels of deubiquitinated substrates such as fatty acid synthase, MDM2, cyclin D1 and Aurora-A."
USP2 affects ARNTL
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USP2 deubiquitinates ARNTL. 1 / 1
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"Accordingly, other investigators have shown that UBP41, a truncated form of USP2, can deubiquitinate BMAL1 in vitro, and that in the presence of USP2b, BMAL1 appears less ubiquitinated and more stable."
USP2 affects ARIH2
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USP2 deubiquitinates ARIH2. 1 / 1
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"Indeed, USP2 but not heat inactivated USP2 depleted the slower migrating, and hence ubiquitylated, form of TRIAD1 (XREF_FIG E)."