IndraLab

Statements


USP47 deubiquitinates YTHDF1. 7 / 7
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"Mechanistically, USP47 prevented YTHDF1 ubiquitination to attenuate the association of YTHDF1 with translation initiation machinery, thereby decreasing m 6 A-based c-Myc translation efficiency."

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"Our immunoblot analyses revealed that overexpression of USP47 with WT ubiquitin or K63-ubiquitin (K63), but not with K48-ubiquitin, inhibited YTHDF1 ubiquitination in HEK293T cells (Figure 6, H and I)."

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"In contrast, catalytically inactive USP47 did not deubiquitinate YTHDF1 in HEK293T cells (Figure 6I)."

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"These data indicate that USP47 prevents YTHDF1 ubiquitination and then attenuates the association of YTHDF1 with the translation initiation machinery in the Tregs."

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"The present study revealed that USP47 prevented the ubiquitination of YTHDF1 and thus prevented its associations with eIF3A to suppress m A-based c-Myc translation in Tregs."

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"Furthermore, deubiquitinase ubiquitin-specific peptidase 47 (USP47) was found to prevent YTHDF1 ubiquitination, thereby disrupting its interaction with the translation initiation machinery and reducing m6A-mediated c-MYC translation efficiency, which is crucial for maintaining Treg cell metabolic and functional homeostasis [80]."

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"USP47 can prevent the ubiquitination of YTHDF1 and reduce its ability to promote translation, thereby exerting control over c-Myc expression."