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USP3 deubiquitinates SMARCA5. 4 / 4
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"Herein, we report one critical target of USP3, SMARCA5 and the specific mechanism of USP3-mediated deubiquitination of SMARCA5 in Docetaxel-inducing DNA damage, suggesting that USP3 may be a promising target for anticancer therapy in prostate cancer.SMARCA5, the SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5, was required for DNA-templated events including transcription, DNA replication, and DNA repair [17, 18]."
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"Firstly, we found USP3 silencing increased SMARCA5 polyubiquitination (Fig. 3J)."
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"Second, ectopic expression of wild-type USP3, but not the C168S mutant, reduced the polyubiquitination of SMARCA5 (Fig. 3K), suggesting that the enzymatic activity of USP3 is indispensable for USP3-dependent deubiquitination of SMARCA5."
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"Taken together, these results suggest that USP3 targets SMARCA5 for stability.As USP3 and SMARCA5 were required for DNA repair [18, 22], which has a key role in human cancer, it is possible that USP3 promotes deubiquitination and stabilization of SMARCA5 in PCa specimens."
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