IndraLab

Statements


PSMD14 deubiquitinates E2F1. 8 / 8
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"This finding led us to hypothesize that POH1 may interact with and deubiquitinate E2F1."

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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 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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"POH1 knockdown significantly enhanced the levels of E2F1 ubiquitination (XREF_FIG)."

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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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"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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"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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"In line with our results, a previous study revealed that POH1, a deubiquitinase, binds to and deubiquitinates E2F1, contributing to its stabilization."