IndraLab

Statements

PPARG binds USP2. 8 / 8
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"To further investigate whether USP2 directly interacts with PPAR-γ, we performed endogenous and exogenous co-immunoprecipitation (Co-IP) analysis."
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"USP2 interacted with PPAR-γ in C2C12 cells and the Gas muscle ( xref )."
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"Further immuno-precipitation analysis and pulldown assay also joined to confirm the interaction between USP2 and PPARγ ( xref )."
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"Targeting the USP2–PPAR-γ axis may offer promising therapeutic strategies for metabolic disorders and sarcopenia."
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"In addition, the computational modeling was used to determine whether USP2 binds to PPARγ and which residues are required for their interaction."
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"Data also showed the USP2-PPAR-γ interaction was key in mediating the effects of USP2 on muscle atrophy and insulin signaling ( xref and xref )."
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"By identifying USP2 as a novel PPAR-γ deubiquitinase and protective factor, we have broadened the PPAR-γ regulatory network and revealed the potential of targeting the USP2–PPAR-γ axis for skeletal muscle and insulin signaling disorders."
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"These findings highlight the potential of targeting the USP2–PPAR-γ axis for therapeutic interventions aimed at combating muscle atrophy and enhancing insulin sensitivity, thereby presenting novel avenues for addressing metabolic disorders and sarcopenia."
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