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USP20 deubiquitinates RETREG1. 10 / 10
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"Additionally, denaturing immunoprecipitation experiments provided evidence that USP20 could still deubiquitinate RETREG1 even when its RHD domain or the C-terminal domain was deleted (Figure S5E)."
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"Deubiquitination of RETREG1 by USP20 promotes its binding with LC3B and consequently enhances reticulophagy."
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"We then investigated the potential role of VAPs in mediating the deubiquitination of RETREG1 by USP20."
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"Surprisingly, even in the absence of the USP20 FFAT motifs, we observed that USP20 was still able to bind to and deubiquitinate RETREG1 (Figure S6A-B)."
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"Our study demonstrates that USP20 deubiquitinates and stabilizes the reticulophagy receptor RETREG1 to facilitate reticulophagy."
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"During this stage, USP20 deubiquitinates RETREG1, stabilizing it and facilitating the recruitment of VAPs, along with early autophagy-related proteins, to the ER subdomain for the initiation of autophagy."
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"USP20 specifically mediates the deubiquitination of the reticulophagy receptor RETREG1."
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"The results indicated that RETREG1 is specifically deubiquitinated by USP20, as the ubiquitination level of RETREG1 significantly decreased under conditions of USP20 overexpression (Figure S4A)."
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"These findings indicate that USP20 participates in the regulation of RETREG1 degradation through the proteasome pathway.Next, we sought to identify the specific sites where USP20 deubiquitinates RETREG1."
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"Furthermore, USP20 was still able to effectively deubiquitinate RETREG1 even in the presence of these mutations."
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