IndraLab

Statements

USP28 binds PPARA. 4 / 4
| 4
sparser
"Mechanistically, USP28 directly interacted with PPARα, deubiquitinated and promoted Mfn2 transcription by stabilizing PPARα (Lys152), finally blocking the morphofunctional defects of mitochondria ( xref )."
39114353
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
"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