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USP9X deubiquitinates KRAS. 4 / 4
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"These results collectively indicate that the 173-345 aa form of NDRG3 can exert a dominant-negative effect on the NDRG3/USP9X-mediated KRAS stabilization process by competing with intact NDRG3 protein for KRAS binding, thereby interfering with the deubiquitination of KRAS by USP9X."
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"It becomes then important in future studies to finely elucidate the structural mechanism of the interaction between KRAS and C-terminal NDRG3, and devise ways to molecularly control it.In conclusion, we showed that KRAS protein is deubiquitinated by USP9X via the scaffolding function of NDRG3, promoting KRAS protein accumulation and KRAS-driven tumorigenesis."
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"KRAS protein is deubiquitinated and stabilized by USP9X (Ubiquitin Specific Peptidase 9 X-Linked) via the scaffolding function of NDRG3."
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"Also, the KRAS ubiquitination level that was highly reduced by USP9X overexpression returned to the normal level upon NDRG3 depletion (Fig. 5j and Supplementary Fig. 6b)."
39819877