IndraLab

Statements

USP9X deubiquitinates TOP3B. 6 / 6
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"Inactivation of USP9X destabilizes TOP3B, and depletion of both TDRD3 and USP9X does not promote further TOP3B ubiquitylation."
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"We also find that USP9X antagonizes TOP3B ubiquitylation by the E3 ligase Mind bomb E3 Ubiquitin Protein Ligase 1 (MIB1)."
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"These results indicate that USP9X deubiquitylates TOP3B only when bound to TDRD3."
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"To confirm the role of TDRD3 in mediating TOP3B deubiquitylation by USP9X, we depleted USP9X in TDRD3KO HCT116 cells."
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"This result confirms that the DUB activity of USP9X is responsible for the stabilization of TOP3B and TDRD3.Altogether, we conclude that USP9X deubiquitylates and stabilizes TOP3B and that TDRD3 acts by mediating the deubiquitylation of TOP3B by USP9X."
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"Although it has been reported that USP9X interacts with, deubiquitylates, and stabilizes TDRD3 and that USP9X is stimulated by TDRD3 , our study reveals that TOP3B is a substrate of USP9X and establishes that USP9X requires TDRD3 to deubiquitylate TOP3B."
37980342