IndraLab

Statements

USP33 is ubiquitinated. 6 / 6
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"Finally, we demonstrate that VDU1 is able to be ubiquitinated via a pVHL-dependent pathway for proteasomal degradation, and VHL mutations that disrupt the interaction between VDU1 and pVHL abrogate the ubiquitination of VDU1."
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"Conversely, it has been reported that β-TrCP promotes the ubiquitination and degradation of deubiquitinase USP33 independently of the DSG motif, despite with the canonical degron motif DSGxxS [ xref ]."
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"Unexpectedly, we found that overexpression of β-TrCP can also increase the ubiquitination of FH-USP33(△DSG) ( Fig. 2 D ), and knockdown of β-TrCP also decreased the ubiquitin[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Here, our study for the first time uncovered that β-TrCP plays the roles in tumor cell proliferation and invasion by promoting ubiquitination and degradation of USP33."
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"USP33 was found to be ubiquitinated in a VHL-dependent manner which targeted it for proteasomal degradation, and VHL mutations that disrupt the protein’s interaction with the DUB abrogated USP33 ubiquitination."
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"Data from the literature indicate that pVHL30 mediates the ubiquitination and degradation of both USP33 and USP20, in turn down-regulating the pathways controlled by these two proteins [ xref ]."
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