IndraLab

Statements

USP14 inhibits USP14. 6 / 7
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"H/R treatment substantially enhanced the expression levels of USP14 mRNA and protein expression (Figure 3A–C), and p‐p65 protein expression (Figures 3B and 3D) in HTR8/Svneo and B6Tert‐1 cell lines.3.4 Depletion of USP14 abrogated H/R-induced upregulation of USP14, p-p65, and proinflammatory cytokines."
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"We found that (i) USP14 could bind to AR, and additionally, both genetic and pharmacological inhibition of USP14 accelerated the ubiquitination and degradation of AR; (ii) downregulation or inhibition of USP14 suppressed cell proliferation and colony formation of LNcap cells and, conversely, overexpression of USP14 promoted the proliferation; and (iii) reduction or inhibition of USP14 induced G0/G1 phase arrest in LNcap prostate cancer cells."
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"Importantly, co-expression of USP14 with mutant MIU1 RNF168, which failed to interact with USP14, prevented USP14 from inhibiting histone Ubn."
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"Our data suggest that the reduction of NFκB activity is a critical consequence of USP14 inhibition and that therapeutic inhibition of USP14 in combination with radiation treatment enhances survival in HNSCC xenograft in vivo in a host TNF-dependent manner."
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"In support of that finding, a small molecule inhibitor of USP14, called IU1, which blocks the catalytic activity of USP14, was found to enhance the in vitro degradation of model proteasome substrates (Lee et al., 2010)."
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"PtPT is also strikingly distinct from IU1, a USP14 inhibitor reported previously [ xref ], which inhibits USP14 but not UCHL5 activity and promotes the degradation of ubiquitinated proteins."
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