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USP7 deubiquitinates AXIN. 11 / 11
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"Coexpression of USP7 suppressed either RNF146 or SIAH1-induced poly-ubiquitination of Axin (Supplementary Fig. 3d)."
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"USP7 deubiquitinates Axin protein, which is a part of a complex that inhibits β-catenin protein."
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"A component of the destruction complex, Axin, is ubiquitinated by RNF146, Smurf1/2, and Siah1 and deubiquitinated by USP7, USP34, and USP44 (Kim and Jho 2010; Lui et al. 2011; Zhang et al. 2011; Fei et al. 2013;  Ji et al. 2017; Ji et al. 2019; Huang et al. 2020)."
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"However, a recent study suggested that USP7 physically deubiquitinated Axin, but not β-catenin, thus serving as a negative regulator of Wnt signaling [ 37 ]."
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"Lei Ji et al. showed that USP7 inhibited Wnt/β-catenin by interacting with Axin TRAF domains and promoting the de-ubiquitination and stabilization of Axin 28."
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"USP7 directly interacts with Axin through its TRAF domain, and promotes deubiquitination and stabilization of Axin."
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"Contrary to our finding, a more recent study showed that USP7 is a potent negative regulator of WNT/β-catenin signaling by deubiquitinating and stabilizing AXIN (Ji et al., 2019), casting doubt on the use of USP7 as WNT inhibitor for patients with APC-mutated CRC."
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"Deubiquitination of Axin mediated by USP7 prevents Axin from degrading and providing stability."
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"USP7 promotes deubiquitination and stabilization of Axin."
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"Our results demonstrated that USP7 and β-catenin exhibited opposite trends; however, it remains unclear how USP7 mediates the deubiquitination of Axin in the absence of Kcnma1 in osteoblasts."
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"These results suggest that polyubiquitinated Axin1, but not β-catenin, is an efficient substrate of USP7.Since USP7 knockout promotes Wnt-induced Axin degradation (Fig. 3d, e), we next examined whether USP7 knockout affects Wnt-induced Axin ubiquitination."
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