IndraLab

Statements

USP46 binds USP12. 28 / 32
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"EBNA3A and EBNA3B target the USP46 and USP12 complexes in LCLs."
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"H. Model : UAF1 mediates the interaction between USP1 and RAD51AP1.of USP12 and USP46, 2 DUBs that also associate with UAF1,26 did not significantly affect the RAD51AP1 stability, suggesting that the effect is specific to the USP1-UAF1 complex.Mapping of the UAF1 interacting region of RAD51AP1In order to specifically determine the functional significance of the UAF1-RAD51AP1 interaction, we sought to identify the residues within RAD51AP1 required for interacting with UAF1."
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"Our data demonstrates a proof-of-principle for USP12 and USP46 complex targeting in PC and uncovers additional mechanisms of galeterone activity."
29861848
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"WDR48, a WD40 repeat-containing protein, interacts with USP12 and USP46 and is required for the histone deubiquitination activity."
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"Similarly galeterone inhibition did not have a significant effect on transcript levels of USP12 and USP46 complex members UAF1 (adj. p = 0.4) and WDR20 (adj. p = 0.25)."
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"Conversely, in the CWR22Rv1 cell line silencing AR FL alone decreased galeterone efficiency by 4 fold compared to SCR control and silencing USP12 or USP12 and USP46 complex members had no significant effect on galeterone efficacy."
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"Although the PHLLP1 and PHLLP2 phosphatases have been reported to be components of the USP46 and USP12 complexes, they were not detectably associated with EBNA3 complexes, likely because these phosphatases are predominantly membrane associated [XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR]."
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"Membrane associated USP46 and USP12 complexes have been implicated in regulating membrane trafficking of receptors, including Notch1 and GLR1 [XREF_BIBR, XREF_BIBR]."
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"We therefore tested C527 for its ability to inhibit the purified USP12 and USP46 complex or other DUBs."
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"C527 inhibited the DUB activity of the USP12 and USP46 complex and other DUB enzymes in vitro."
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"PHLPP1, histone H2A, and H2B have been identified as substrates of both USP12 and USP46, suggesting that USP12 and USP46 are associated with AKT signaling in cancer cells and transcription activation in Xenopus embryo [ xref , xref , xref ]."
39482856
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"The mode of interaction of USP12 and USP46 with UAF1 is still unclear."
23797609
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"Galeterone binds to USP12 and USP46."
29861848
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"BIAcore SPR studies demonstrated a dose dependent binding of galeterone to USP12 and USP46 (Figure xref )."
29861848
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"To understand further the nature of the USP12 and USP46 complexes, we attempted to identify proteins that interact with the USP12 and USP46 deubiquitinating enzyme complexes."
20147737
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"UAF1 also binds and activates two other DUBs, USP12 and USP46 ( xref ), and studies that reveal how UAF1 binds and activates USP12 and USP46 suggest that UAF1 will bind to USP1 in an analogous manner ( xref , xref )."
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"Biochemical and proteomic studies showed that two WDR proteins, WDR48 (also known as USP1-associated factor, UAF1) and WDR20, interact with USP46 and USP12 (Cohn et al., xref ; Sowa et al., xref ; Kee et al., xref )."
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"It also lacks the binding site for another activator, WDR20, which binds USP12 and USP46, leading to further activation (Kee et al , xref )."
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"Besides the above studies, in virus infection, EBV nucleoproteins EBNA3A, EBNA3B, and EBNA3C were found to be highly associated with the USP46-USP12 complex, and EBNA3A and EBNA3C are essential for EBV-mediated transformation of resting B lymphocytes into immortalized lymphoblastoid cell lines (LCL) [ xref ]."
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"Together, these structural studies suggest that binding of the WDR proteins to USP12 or USP46 relatively far from the active site results in the rearrangement of several structural elements, which propagates to the catalytic triad increasing enzyme catalysis."
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"The more distantly related USP1 is also regulated by WDR48, but WDR20 is unique to USP12 and USP46 complexes."
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"The unique binding mode elucidated here thus provides a framework to guide further exploration into the role of the larger USP1 insertions and the particular interactions of USP12 and USP46 in mediati[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26388029
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"Our experiments revealed that the DUBs USP12 and USP46 complexed with WDR48 and WDR20 remove ubiquitin from the cytoplasmic tails of internalized Itgb1 and several other cells surface proteins including signaling proteins and solute transporters, resulting in a decoupling from ESCRT-mediated degradation."
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"Next, we isolated biotinylated proteins from cell lysates with streptavidin-conjugated beads, performed MS, and identified USP46, the paralog USP12, and the USP12- and USP46-binding and activating adapter proteins WDR48 and WDR20 (Li et al, 2016; Zhu et al, 2019) (Fig. 1C)."
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"We did not detect any USP1 peptides in our complexes, suggesting that the even though the EBNA3 proteins interact strongly with WDR48, they are selective for USP12 and USP46 complexes, possibly due to stabilizing interactions with WDR20 or the enzymes themselves."
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"Besides the above studies, in virus infection, EBV nucleoproteins EBNA3A, EBNA3B, and EBNA3C were found to be highly associated with the USP46-USP12 complex, and EBNA3A and EBNA3C are essential for EBV-mediated transformation of resting B lymphocytes into immortalized lymphoblastoid cell lines (LCL) [100]."
37752518
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"To understand further the nature of the USP12 and USP46 complexes, we attempted to identify proteins that interact with the USP12 and USP46 deubiquitinating enzyme complexes."
20147737
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"The cDNAs encoding catalytically inactive USP12 and USP46 and binding deficient USP12 , USP12 , USP12 , WDR48 , and WDR20 were generated by site-directed mutagenesis and cloned into pEGFP-C1 and pRetroQ-C1 vectors (Clontech)."
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