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USP43 deubiquitinates MYC. 3 / 3
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"These results suggest that wild-type USP43 primarily stabilizes c-Myc by directly deubiquitinating c-Myc, while USP43 with a loss of catalytic activity still protects c-Myc to some extent by competitively binding to c-Myc with FBXW7."
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"Next, the type of polyubiquitin chain of c-Myc deubiquitinated by USP43 was examined, and our data indicated that USP43 catalyzed the deubiquitination of the K48 chain but not the K63 chain of c-Myc, which is associated with proteasomal pathway degradation [28] (Fig. 5H)."
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"Further deubiquitination assays showed that USP43 was able to deubiquitinate wild-type c-Myc but not the c-Myc mutants K148R, K289R, and K148/289R (Fig. 5J)."
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