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USP36 deubiquitinates DGCR8. 1 / 1
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"Indeed, although we did observe the marginal ubiquitination of exogenously expressed DGCR8 that can be deubiquitinated by WT USP36, but not the catalytically-inactive C131A mutant (Supplementary Fig. S4A), the levels of endogenous DGCR8 ubiquitination are below detectable (Supplementary Fig. S4B), suggesting that the steady-state levels of DGCR8 ubiquitination under normal cell growth conditions are too low to be regulated by USP36."