Neglected PTM in animal adipogenesis: E3-mediated ubiquitination

Ubiquitination is a widespread post-transcriptional modification (PTM) that occurs during protein degradation in eukaryotes and participates in almost all physiological and pathological processes, including animal adipogenesis. Ubiquitination is a cascade reaction regulated by the activating enzyme E1, conjugating enzyme E2, and ligase E3. Several recent studies have reported that E3 ligases play important regulatory roles in adipogenesis. However, as a key influencing factor for the recognition and connection between the substrate and ubiquitin during ubiquitination, its regulatory role in adipogenesis has not received adequate attention. In this review, we summarize the E3s' regulation and modification targets in animal adipogenesis, explain the regulatory mechanisms in lipogenic-related pathways, and further analyze the existing positive results to provide research directions of guiding significance for further studies on the regulatory mechanisms of E3s in animal adipogenesis.

Automated summary

Ubiquitination, a post-transcriptional modification, plays a crucial role in protein degradation and is involved in various physiological and pathological processes, including animal adipogenesis. The E3 ligases have been found to regulate adipogenesis, but their role in the recognition and connection between substrate and ubiquitin during ubiquitination has been overlooked. This review summarizes the regulatory and modification targets of E3 ligases in animal adipogenesis, explains the regulatory mechanisms in lipogenic pathways, and analyzes existing positive results, providing valuable research directions for further understanding the regulatory mechanisms of E3 ligases in animal adipogenesis.