IndraLab

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USP22 binds PPARG. 8 / 12
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"For instance, the USP22-PPARγ axis plays a significant role in modulating both adipogenesis and inflammation, whereas disorders in bile acid metabolism and alterations in gut microbiota exhibit bidirectional regulation. xref In light of these mechanisms, preclinical studies have led to the development of small-molecule inhibitors that target USP22 and FXR."
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"In vitro pulldown assays with purified recombinant proteins demonstrated that USP22 directly bound to PPARγ (Fig.  xref )."
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"We subsequently performed coimmunoprecipitation experiments to confirm the interaction between USP22 and PPARγ (Fig.  xref ), and predicted their possible binding sites via HDOCK software (Fig.  xref )."
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"Then, the specific interaction between USP22 and PPARγ was confirmed by co-immunoprecipitation assay with exogenously transduced USP22 and PPARγ in HEK293T cells (Fig.  xref )."
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"Overall, our results confirm that USP22 specifically interacts with PPARγ, which is a key transcription factor related to lipid metabolism."
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"Interestingly, we found that USP22 strongly bound to the PPARγ DBD domain (Fig.  xref ) as well as pVHL and CUL4B proteins in the HCC cells (Supplementary Fig.  xref ), and the interaction between PPARγ and USP22 significantly decreased the pVHL and CRL4B AhR involved ubiquitination (Fig.  xref ), indicating that USP22 regulates deubiquitination of PPARγ through other lysine sites."
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"Taken together, these results indicate that USP22 directly interacts with PPARγ and functions as a bona fide PPARγ deubiquitinase in cells."
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"Mechanistically, USP22 bound to peroxisome proliferator-activated receptor gamma (PPARgamma) and inhibited its ubiquitination, thereby stabilizing PPARgamma and promoting efferocytosis."
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