IndraLab

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USP1 binds KDM4A. 22 / 22
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"Our above findings suggest that targeting the USP1‐KDM4A axis could antagonize the growth of PC cells."
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"23, 24 To test whether WDR48 is required for the interaction between KDM4A and USP1, we undertook coimmunoprecipitation experiments in RV1 cells using KDM4A or WDR48 Ab pull-down assays."
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"In addition, the association of endogenous KDM4A with USP1 was reduced by WDR48 knockdown treatment in RV1 cells (Figure  xref )."
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"Overall, these findings revealed that c‐Myc was a key downstream effector of the USP1‐KDM4A axis to drive the growth and survival of PC cells."
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"The interaction between KDM4A and USP1 was confirmed by coimmunoprecipitation experiments in 293T cells overexpressing KDM4A."
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"The interaction of USP1 and KDM4A led us to test a potential role for the ubiquitination enzyme USP1 in the regulation of KDM4A turnover and function."
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"Collectively, we showed that USP1 interacts with KDM4A and promotes its deubiquitination, ultimately leading to KDM4A stabilization, and inhibition of USP1 promotes the response of PC cells to therapeutic agent enzalutamide."
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"In addition, in our study, USP1 directly binds and stabilizes KDM4A but does not affect its transcription, suggesting deubiquitination is the major regulation of KDM4A by USP1."
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"To evaluate the possible involvement of the USP1‐KDM4A axis in modulating c‐Myc expression."
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"Taken together, these results indicate that USP1 promotes the expression of c‐Myc by regulating KDM4A. We next asked how the USP1‐KDM4A axis increases AR‐dependent c‐Myc transcription."
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"The interaction between KDM4A and USP1 was confirmed by coimmunoprecipitation experiments in 293T cells overexpressing KDM4A (Figure  xref )."
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"Multiple reports showed WDR48 act as a strong activator of USP1 by enhancing the USP1‐mediated deubiquitination. xref , xref To test whether WDR48 is required for the interaction between KDM4A and USP1, we undertook coimmunoprecipitation experiments in RV1 cells using KDM4A or WDR48 Ab pull‐down assays."
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"As is well known, active transcription foci are distributed in the nucleus in a punctate pattern; therefore, USP1, WDR48, KDM4A, and AR might form a complex to regulate transcription in PC cells."
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"Collectively, we showed that USP1 interacts with KDM4A and promotes its deubiquitination, ultimately leading to KDM4A stabilization, and inhibition of USP1 promotes the response of PC cells to therapeutic agent enzalutamide (Figure  xref )."
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"To determine whether the USP1‐KDM4A axis‐dependent transcription of c‐Myc requires the AR ligand, we maintained the PC cells (control, shUSP1, and shUSP1 + KDM4A) in the media supplemented with CS FBS that contains extremely low levels of androgen for 2 days, followed by treatment of cells with or without synthetic androgen R1881 for 1 day."
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"3.3 USP1 binds and stabilizes KDM4A."
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"To determine whether KDM4A and USP1 directly interact, we mixed the purified GST‐USP1 with the purified Flag‐KDM4A and tested the in vitro binding between the 2 proteins."
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"Taken together, our results reveal that the USP1‐KDM4A axis is required for the constitutive association between AR and c‐Myc enhancer in the presence or absence of androgen."
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"USP1 binds and stabilizes KDM4A."
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"In addition, in our study, USP1 directly binds and stabilizes KDM4A but does not affect its transcription, suggesting deubiquitination is the major regulation of KDM4A by USP1."
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"The interaction of USP1 and KDM4A led us to test a potential role for the ubiquitination enzyme USP1 in the regulation of KDM4A turnover and function."
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"c‐Myc is a downstream effector of USP1‐KDM4A axis in PC cells."
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