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PSMD14 deubiquitinates E2F1. 17 / 17
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"Similarly, in head and neck squamous cell carcinoma (HNSCC), PSMD14 decreased E2F1 ubiquitination and degradation, which improved AKT pathway activation and SOX2 transcription, thereby facilitating HNSCC growth, chemoresistance, and stemness [48]."
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"In line with our results, a previous study revealed that POH1, a deubiquitinase, binds to and deubiquitinates E2F1, contributing to its stabilization."
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"PSMD14 mediates deubiquitination and stabilization of E2F1 preventing its proteasomal degradation [ 45 , 62 ]."
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"By deubiquitinating and stabilizing E2F1, PSMD14 effectively promotes tumor formation in liver cancer [ 31 ]."
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"It is reported that the E2F1 is also deubiquitinated and stabilized by POH1 (a deubiquitinating enzyme) [ 52 ]."
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"POH1 knockdown significantly enhanced the levels of E2F1 ubiquitination (XREF_FIG)."
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"This finding led us to hypothesize that POH1 may interact with and deubiquitinate E2F1."
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"In addition, in MG132 treated cells, wherein the global proteasomal activity was inhibited, ectopic POH1 expression was able to deubiquitinate E2F1 (XREF_SUPPLEMENTARY), suggesting that this effect is independent of the overall proteasome function."
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"Our present study provides evidence that POH1 deubiquitinates and stabilizes the master transcription factor E2F1 and functions as a tumour promoting protein in HCCs."
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"We demonstrated that POH1 efficiently deubiquitinates E2F1 by removing the K-63 polyubiquitin chains, and this observation is consistent with previous studies revealing that the JAMM domain within POH1 is responsible for removing K63 linked ubiquitin chains XREF_BIBR XREF_BIBR XREF_BIBR."
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"Of note, although E2F1 deubiquitination by POH1 has been revealed to be important for E2F1 stabilization, the molecular details of the regulation remain to be defined."
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"We propose that the deubiquitination of E2F1 by POH1 primarily occurs in the nucleus; as a consequence, the prosurvival genes, including Survivin and FOXM1, are transcriptionally activated."
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"E2F1 is also deubiquitinated and stabilized by a deubiquitinating enzyme named POH1 (43)."
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"Similarly, in HCC, PSMD14 deubiquitylates transcriptional factor E2F1, increases its stability, and strengthens its downstream pro-survival signals, including upregulation of survivin and FOXM1 expres[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The upregulation of POH1 promotes tumor formation by deubiquitinating and stabilizing the transcription factor E2F transcription factor 1 (E2F1) in liver cancer [ 26 ]."
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"It is reported that POH1/RPN11 (PSMD14), a component of the 19S proteasomal subunit, deubiquitylates E2F1 to prevent its degradation to promote hepatocellular carcinoma (HCC) (Wang et al., 2015)."
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"Mechanistically, PSMD14 increased E2F1 stabilization by binding to and deubiquitinating E2F1."
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