IndraLab

Statements


VCPIP1 activates X. 9 / 9
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"Although VCPIP1 overexpression led to significantly increased HBx in the Huh7 and HepG2 cells, it did not redice the amounts of HBx ubiquitination (Fig. 4C)."

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"RNA interference (RNAi) targeting endogenous PSMC3 was used to validate that PSMC3 was required for VCPIP1-mediated HBx stability but was not a contributing factor."

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"Collectively, the results indicate that VCPIP1-recruited PSMC3 associating with HBx functionally prevents the HBx degradation by the 20S proteasome."

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"As expected, ectopic VCPIP1 expression led to significantly increased HBx in a dose-dependent manner in both Huh7 and HepG2 cells (Fig. 2B)."

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"Then, the similar effects of VCPIP1 and its C-terminal truncation increasing the HBx expression were validated in HepG2.2.15 cells (Fig. 2G), but HBx was reduced by silencing endogenous VCPIP1 (Fig. 2H)."

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"VCPIP1 increases HBx stability.."

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"VCPIP1 inhibits HBx degradation through the proteasome pathway in a ubiquitin-independent manner.."

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"PSMC3 , encoding the 26S proteasome regulatory subunit , directly stabilized HBx through physical binding instead of a common approach in protein degradation , serving as the key downstream effector of VCPIP1 on HBx ."

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"Finally, the VCPIP1-induced HBx stability greatly promoted its canonical transcriptional activities and contributed to the inhibition of colony formation of Huh7 and HepG2 cells."