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PSMD14 activates E2F1. 14 / 19
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"Accordingly, depletion of Poh1 in poh1 f/f MEFs could cause an acceleration of E2F1 protein turnover that apparently was not due to the change in E2F1 mRNA levels (XREF_SUPPLEMENTARY)."
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"POH1 overexpression positively regulated E2F1 activity, as monitored by an E2F1 binding element-luciferase reporter, whereas POH1 deletion yielded an opposite effect (XREF_FIG)."
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"Overexpression of the K63 resistant form of ubiquitin (K63R) attenuated POH1 knockdown induced E2F1 downregulation, indicating that K63 linked polyubiquitination is important for POH1 mediated E2F1 turnover (XREF_FIG)."
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"XREF_BIBR proposed that the aberrant upregulation of nuclear POH1 mediated E2F1 stabilization promotes tumor formation in hepatocellular carcinoma (HCC)."
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"In summary, we propose that the aberrant upregulation of nuclear POH1 mediated E2F1 stabilization is an important event in the development of liver cancer and that targeting POH1 might serve as a promising strategy for cancer treatment."
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"The results indicate that forced POH1 expression significantly potentiates E2F1 protein stability (XREF_FIG)."
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"Furthermore, we generated different siRNA resistant (siR-R) POH1 constructs for rescue assays, and the results showed that restoration of POH1 expression with the C120S-, H113Q- and DeltaJAMM POH1 mutants did not attenuate the inhibition of E2F1 caused by the deletion of endogenous POH1 (XREF_FIG)."
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"Moreover, PSMD14 mediated E2F1 stabilization could promote tumor formation in liver cancer XREF_BIBR."
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"Therefore, our data indicate that PSMD14 mediated increase of E2F1 directly promotes the transcription activation of SOX2."
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"Through immunoblotting assay , we confirmed that PSMD14 blocking inhibited the expression of E2F1 ( Figure 5A ) , while no obvious change was found in E2F1 mRNA level ( Figure S5 ) ."
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"Briefly, PSMD14 suppressed the degradation of E2F1, and then E2F1 promoted AKT and SOX2 positive feedback loop."
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"Although POH1 overexpression caused the deubiqutination of E2F1, the approach did not have an appreciable impact on levels of total polyubiquitin modified proteins (XREF_SUPPLEMENTARY), suggesting that POH1 mediated deubiquitination of E2F1 can take place in cells in absence of a noticeable alteration in global proteasome activity."
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"The deubiquitination of E2F1-K63 polyubiquitin chains appears to be important for POH1 mediated stabilization of E2F1 because Ub-K63R overexpression showed a dominant negative effect that rescued E2F1 expression in cells with POH1 inhibition (XREF_FIG)."
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"Then, we validated that the ubiquitination level of E2F1 was greatly elevated in HNSCC cells stably transfected with shPSMD14, indicating that PSMD14 prevented the degradation of E2F1 through ubiquitin-proteasome system (UPS)."
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