IndraLab

Statements

USP28 binds PPARA. 5 / 5
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"RNA sequencing, immunoprecipitation and mass spectrometry analysis, chromatin immunoprecipitation assays, chromatin immunoprecipitation sequencing, and protein pull-down assay mechanistically revealed that USP28 directly interacted with PPARα (peroxisome proliferator-activated receptor α), deubiquitinating and stabilizing PPARα (Lys152) to promote Mfn2 (mitofusin 2) transcription, thereby impeding mitochondrial morphofunctional defects."
37994595
sparser
"Mechanistically, USP28 directly interacts with PPARα, deubiquitinates and stabilizes it at Lys152, promoting transcription of Mfn2 to restore mitochondrial fusion, which mitigates ROS production, reduces fibrosis, and improves both systolic and diastolic function in models of diabetic cardiomyopathy [ xref ]."
41382274
sparser
"Moreover, a recent study has demonstrated that USP28 can directly interact with PPARα (Lys152) and exert a protective effect in DCM by regulating mitochondrial homeostasis through the PPARα-Mfn2 axis."
38664790
sparser
"Also, we did not find the potential PPARα-USP28 interaction in TAC-induced mouse heart from our LC-MS/MS dataset."
39431010
sparser
"Mechanistically, USP28 directly interacted with PPARα, deubiquitinated and promoted Mfn2 transcription by stabilizing PPARα (Lys152), finally blocking the morphofunctional defects of mitochondria ( xref )."
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