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SPI1 binds USP22. 10 / 13
3 | 5 5
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"In line with the truncated mutant of USP22, the C-terminal ubiquitin-specific peptidase domain of USP22 containing a point mutation could bind SPI1 weakly, whereas the N-terminal zinc finger domain of USP22 containing a point mutation could bind SPI1 more strongly (Fig.  xref )."
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"These results indicate that USP22 interacts with SPI1 and enhances SPI1 stability through deubiquitination."
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"Co-IP assays were then performed to verify the interaction between USP22 and SPI1."
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"The C-terminal ubiquitin-specific peptidase domain of USP22 binds SPI1 strongly, whereas the N-terminal zinc finger domain binds SPI1 weakly (Fig. 5d)."
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"In line with the truncated mutant of USP22, the C-terminal ubiquitin-specific peptidase domain of USP22 containing a point mutation could bind SPI1 weakly, whereas the N-terminal zinc finger domain of USP22 containing a point mutation could bind SPI1 more strongly (Fig. 5g)."
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"Thus, the C-terminal ubiquitin-specific peptidase domain of USP22 is the dominant regulator of binding between USP22 and SPI1."
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"Co-IP assays were performed to determine the interaction between USP22 and SPI1."
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"USP22 interacts with SPI1."
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"Co-IP assays were then performed to verify the interaction between USP22 and SPI1."
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"To identify the region within USP22 interacting with SPI1, we generated two truncated mutants of USP22 in HEK-293T cells."
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