IndraLab

Statements

USP14 deubiquitinates AR. 7 / 7
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"USP14 inhibits AR ubiquitination and subsequent degradation in both prostate and breast cancer cells [77, 78]."
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"Treatment of control MDA-MB-453 (either scramble shRNA or parental) cells with CHX for up to 12h caused decreased levels of AR, suggesting a contribution of AR protein synthesis to endogenous AR protein levels; however, co-treatment of CHX and USP14 shRNA or IU1 resulted more rapid decrease in levels of endogenous AR protein, strongly suggest that deubiquitination of AR protein by USP14 is essential for its protein stability."
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"As a deubiquitinating enzyme, USP14 has previously been reported to enhance the deubiquitination of AR and resist the binding of MDM2, but the specific mechanism is still unclear and needs further exploration."
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"In addition, reduction of UCHL5 by its siRNA did not affect the expression of AR, suggesting that USP14 but not UCHL5 recruited on the19S proteasome plays a selective role in the deubiquitination of AR."
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"We found that IU1 and USP14 knockdown dramatically increased levels of ubiquitinated and K48 ubiquitinated AR, suggesting that USP14 is an AR DUB, capable of deubiquitinating and thereby stabilizing AR protein."
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"Additionally, both genetic and pharmacological inhibition of USP14 significantly suppressed cell proliferation in AR-responsive breast cancer cells by blocking G0/G1 to S phase transition and inducing apoptosis."
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"Moreover, AR overexpression inhibited USP14 inhibition induced events, suggesting that AR deubiquitination by USP14 is critical for breast cancer growth and USP14 inhibition is a possible strategy to treat AR positive breast cancer."
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