IndraLab

Statements

WDR20 binds USP46 and WDR48. 11 / 11
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"These results indicate that USP46 does not associate with its accessory factor UAF1 or WDR20 when interacting with or deubiquitinating Cdt2 in high risk E6 transformed cells."
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"USP46 is normally associated with its accessory proteins UAF1 and WDR20."
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"Figure 1: Model of USP46 bound to WDR48 and WDR20."
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"Together with data showing that co-expression of the USP-46, WDR-48, and WDR-20 complex reduces levels of ubiquitinated GLR-1, these results support a model wherein USP-46, when bound to WDR-48 and WDR-20, deubiquitinates GLR-1 and increases receptor stability and function in vivo."
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"Because USP46 and USP12 are highly homologous (~ 90% identity) and we could confirm a robust association with USP46 by Western blotting (discussed below), we chose to focus our subsequent attention on the USP46, WDR48, and WDR20 complex."
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"Total levels of WDR48 and USP46 were unchanged upon 4HT withdrawal (XREF_FIG) thus increased signal in the WDR48 ChIP at the p14 was not attributable to increased expression of the constituents of the USP46, WDR48, and WDR20 complex by EBNA3C."
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"USP12 and USP46 exhibit the conserved USP fold structure comprised of Fingers, Palm and Thumb subdomains, with the catalytic triad of cysteine, histidine and aspartic acid, nestled in between the Palm and Thumb FIGURE 1 | Model of USP46 bound to WDR48 and WDR20."
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"These recent structural and biochemical studies complement in vivo studies of the USP-46, WDR-48, and WDR-20 complex in C. elegans."
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"Together with data showing that co-expression of the USP-46/WDR-48/WDR-20 complex reduces levels of ubiquitinated GLR-1 (Dahlberg and Juo, 2014), these results support a model wherein USP-46, when bound to WDR-48 and WDR-20, deubiquitinates GLR-1 and increases receptor stability and function in vivo.Interestingly, Huo et al. (2015) showed that knock-down of mammalian USP46 has a greater effect on reducing surface GluA1 (42% decrease) and mEPSC amplitude (32% decrease) than overexpression of USP46 (18%–20% increase in surface GluA1 and mEPSC amplitudes; Huo et al., 2015)."
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"Because our TAP lysis procedure extracted both nuclear and cytoplasmic proteins (XREF_SUPPLEMENTARY), we wanted to ensure that the USP46, WDR48, and WDR20 complex subcellular localization was compatible with formation of a complex with EBNA3 proteins."
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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.These recent structural and biochemical studies complement in vivo studies of the USP-46/WDR-48/WDR-20 complex in C. elegans."
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