IndraLab

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USP11 deubiquitinates TGFBR2. 7 / 8
1 | 7

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"TGFBR2 is deubiquitinated by USP11 to maintain the TGF-β signal pathway (Jacko et al., 2016) and the glycosylation of TGFBR2 enhances the radio-resistance and BC cell stemness (Sun et al., 2021); therefore, maintaining a normal TGF-β pathway is essential for cancer cell control."

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"The novel finding in this study is that USP11 de-ubiquitinates and stabilizes TbetaRII."

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"We demonstrate that knockdown of USP11 increases the ubiquitination of TbetaRII, whereas overexpression of USP11 greatly decreases ubiquitination of TbetaRII."

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"USP11 de-ubiquitinates and stabilizes TbetaRII."

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"Together, these data suggest that deubiquitination of TGFBR2 by USP11 effectively spares TGFBR2 from proteasomal degradation to promote EMT and metastasis."

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"We conducted Co-IP experiments, which revealed that Usp11 was able to interact with Tgfbr2, and inhibition of Usp11 increased the ubiquitination of Tgfbr2."

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"Usp11 promotes the development of renal fibrosis by deubiquitinating Tgfbr2, reducing Tgfbr2 ubiquitination degradation, and then facilitating the activation of downstream senescent signaling pathway."