Modification of RNF183 via m6A Methylation Mediates Podocyte Dysfunction in Diabetic Nephropathy by Regulating PKM2 Ubiquitination and Degradation.

Diabetic kidney disease (DKD) is a prevalent complication associated with diabetes in which podocyte dysfunction significantly contributes to the development and progression of the condition. Ring finger protein 183 (RNF183) is an ER-localized, transmembrane ring finger protein with classical E3 ligase activity. However, whether RNF183 is involved in glomerular podocyte dysfunction, which is the mechanism of action of DKD, is still poorly understood.

FBXW7 mediates high glucose-induced epithelial to mesenchymal transition via KLF5 in renal tubular cells of diabetic kidney disease.

F-box and WD repeat domain-containing 7 (FBXW7) protein is known as one of the crucial components of the E3 ubiquitin ligase called the Skp1-Cullin1-F-box (SCF) complex, which regulates the degradation of a network of proteins via the ubiquitin-proteasome system. In our study, we investigated the latent impact of FBXW7 on renal tubular cells injury and its molecular mechanism in diabetic kidney disease (DKD). FBXW7 was upregulated in kidneys of diabetic mice and human renal proximal tubular cells exposed to high glucose.