IndraLab

Statements


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"These findings imply that the complex formation and USP46 activity regulation are significantly influenced by the residues participating in the USP46-WDR20 interaction ( xref ). xref "

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"The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the deubiquitinating enzyme USP-46 to promote the abundance of the glutamate receptor GLR-1 in the ventral nerve cord of Caenorhabditis elegans."

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"We propose that WDR-20 and WDR-48 form a complex with USP-46 and stimulate the DUB to deubiquitinate and stabilize GLR-1 in vivo."

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"Together, these results indicate that the amino-terminal 1 MEIL 4 motif is necessary for the efficient recruitment of USP12/WDR20 to the PM, but is not sufficient to confer PM localization to a USP46/[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"WDR20 binding to USP12 and USP46 showed a significant increase in the catalytic activity in vitro [71,76]."

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"Besides, USP12 and USP46 can also bind with WDR20 but USP1 cannot; and the activity of USP12 and USP46 can be activated by WDR48 and WDR20 independently and synergistically [38, 39]."

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"This observation suggests that, in the absence of a strong NLS in USP12, recruitment to the PM largely prevails over slow diffusion into the nucleus upon formation of a USP12/WDR20 complex.On the othe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Image analysis showed that the nuclear to cytoplasmic ratio of YFP-USP46 was significantly higher when expressed with Myc-WDR20 NESm than with wild type Myc-WDR20 (Additional File 4b), suggesting that[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Mechanistically, USP46 can bind with WD40-repeat (WDR) proteins WDR-20 and WDR-48 to stimulate USP46 catalytic activity and increase GLR-1 levels."