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USP27X binds CBX2. 16 / 16
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"Our findings indicate that USP27X truncating mutants lacking the USP domain do not bind CBX2, and that absence of the D1 domain in CBX2 disrupts the binding between USP27X and CBX2 (Fig. 1I–L)."
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"Therefore, the interaction between USP27X and CBX2 requires the presence of the USP domain in USP27X and the D1 domain in CBX2."
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"The interaction between USP27X and CBX2 suggests that USP27X may act as a deubiquitinating enzyme targeting the degradation of CBX2 protein."
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"The upregulation of GSK3β in BT549 cells intensified the association between endogenous USP27X and CBX2 (Fig. 5F), whereas the downregulation of GSK3β in MDA-MB-231 and MCF7 cells weakened the interaction between endogenous USP27X and CBX2 (Fig. 5G, H)."
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"For example, glycogen synthase kinase 3 beta (GSK3β) can directly bind to and phosphorylate USP27X, thereby enhancing the interaction between USP27X and CBX2 (Xing et al. 2023)."
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"Furthermore, it has been revealed that glycogen synthase kinase 3 beta (GSK3beta) can directly bind to and phosphorylate USP27X, thereby enhancing the interaction between USP27X and CBX2 and leading to further stabilization of the CBX2 protein."
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"The PLA signal for a direct interaction between exogenous USP27X and CBX2 was detected in HEK-293T cells (Supplementary Fig. 1E)."
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"Subsequently, the interaction between USP27X and CBX2 was validated in HEK-293T cells (Supplementary Fig. 1C)."
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"The interaction between exogenous USP27X and CBX2 was also verified by immunofluorescence assay in HEK-293T cells (Supplementary Fig. 1D)."
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"Furthermore, we observed PLA signaling in the nucleus and cytoplasm, providing additional evidence for a direct interaction between endogenous USP27X and CBX2 (Fig. 1F)."
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