IndraLab

Statements

USP35 binds BRD4. 9 / 9
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"Mechanistically, USP35 interacted with, deubiquitinated, and stabilized BRD4."
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"To further examine how USP35 regulates BRD4 protein level, we performed immunoprecipitation analysis to examine whether there is an interaction between USP35 and BRD4."
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"Our study uncovers that USP35 interacts with and deubiquitinates BRD4, and enhances SLC7A11 expression in ER+ breast cancer."
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"To further examine how USP35 regulates BRD4 protein level, we performed immunoprecipitation analysis to examine whether there is an interaction between USP35 and BRD4."
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"Immunoprecipitation data showed that Flag-tagged BRD4 interacted with USP35 in transiently transfected 293T17 cells (Fig.  xref )."
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"Together, our results demonstrate that USP35 interacts with BRD4, and regulates BRD4 protein level by increasing BRD4 protein stability through deubiquitination in ER+ breast cancer cells."
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"Considering that BRD4 interacts with USP35, and regulates SLC7A11 level, we hypothesized that USP35 via BRD4 regulates SLC7A11 level and ferroptosis in ER+ breast cancer cells."
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"Furthermore, USP35 did not interact with BRD4 in TNBC cells (Supplementary Fig.  xref ), suggesting that USP35 inhibited ferroptosis independent of the BRD4-SLC7A11 axis in TNBC although BRD4 and SLC7A11 mRNA levels were positively correlated (Supplementary Fig.  xref ), which was different from in ER+ breast cancer (Fig.  xref )."
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"Since USP35 also interacted with BRD4 (Fig.  xref ), it is possible that BRD4 together with USP35 and/or ERα regulate the transcription of SLC7A11 , conferring resistance to ferroptosis in ER+ breast cancer cells, which could explain why BRD4 partially rescued SLC7A11 expression in USP35 knockdown ER+ breast cancer cells (Fig.  xref )."
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