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Statements

USP22 binds SNAI1. 11 / 11
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"WB results showed that the mutation of lysine residues in C-terminal or N-terminal had no effect on the binding of USP22 and Snail1 ( Fig. 8 C)."
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"Despite the mutation of lysine residues in C-terminal or N-terminal having no effect on the binding of USP22 and Snail1, the WT Snail1 and the Snail1(C-8KR) mutant plasmid could decrease the ubiquityl[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Therefore, the USP22-Snail1 signal axis may be a new target for delaying diabetes TIF. (i) EMT induced by HG can promote TIF, which is one of the main pathological changes induced by DN."
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"Co-IP experiment results also showed that USP22 could bind to Snail1 in NRK-52E cells ( Fig. 7 C), and HG stimulation obviously increased their interactions ( Fig. 7 C)."
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"We further performed Co-IP experiment to determine whether the mutation of lysine residues in C-terminal and N-terminal affected the binding between USP22 and Snail1."
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"Further study found that quercetin inhibited the interaction between USP22 and Snail1, thereby reducing the stability of Snail1."
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"Further study found that quercetin inhibited the interaction between USP22 and Snail1, thereby reducing the stability of Snail1."
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"Despite the mutation of lysine residues in C-terminal or N-terminal having no effect on the binding of USP22 and Snail1, the WT Snail1 and the Snail1(C-8KR) mutant plasmid could decrease the ubiquityl[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Co-IP experiment results also showed that USP22 could bind to Snail1 in NRK-52E cells ( Fig. 7 C), and HG stimulation obviously increased their interactions ( Fig. 7 C)."
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"Co-IP assay was used to verify whether USP22 and Snail1 can interact with each other."
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"When over-expressed, USP22 interacts with and stabilizes Snail1; however, the fact USP22 cannot compensate the lack of USP27X (in terms of Snail1 stability) suggest USP27X has a predominant role in Snail1 stabilization [5]."
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