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USP9X leads to the deubiquitination of KDM4C. 4 / 4
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"The deubiquitinase USP9X increases radiotherapy resistance of lung malignancy by promoting KDM4C deubiquitination and activating the TGF-β2/Smad pathway [ 36 ]."
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"Our previous study found that the deubiquitinase USP9X could interact with the histone lysine demethylase 4 C (KDM4C) to mediate KDM4C deubiquitination and thus upregulate its protein expression, and aberrantly expressed KDM4C upregulated the transcriptional expression of TGF-β2 by directly reducing the level of histone H3K9me3 in the promoter region of TGF-β2, which in turn activated the Smad/ATM/Chk2 signaling pathway, promoting DNA damage repair and leading to lung cancer radioresistance [19]."
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"Using tandem affinity purification technology, we further identify deubiquitinase <span class="match term0">USP9X</span> as a critical binding partner that deubiquitinates and stabilizes <span class="match term1">KDM4C</span>"
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"USP9X enhances the deubiquitination of KDM4C to elevate radioresistance of lung cancer cells by activating the TGF‐β2/Smad signaling [12]."
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