Ubiquitin Proteins and the Orchestration of Transcription Factors Activity

The ubiquitin proteasome system is a key pathway, regulating targeted proteins degradation. A critical step is regulated by E3 ubiquitin ligases, which facilitates the transfer of ubiquitin moieties to substrate proteins, leading proteins degradation via 26S proteasome. However, the number of known ubiquitin dependent processes is still relatively small. Since some stress-related transcription factors are usually essential under stress conditions, while playing negative roles during normal growth, hence their protein levels need to be precisely regulated. However, the mechanism of ubiquitin pathway, regulating transcription factors stability has not been yet summarized. In this review, we attempted to outline the mechanism of E3 ligases dependent transcription factors degradation and discuss the comprehensive role of E3 ligases in phytohormone signaling.

Automated summary

The ubiquitin proteasome system plays a crucial role in targeted protein degradation, with E3 ubiquitin ligases facilitating the transfer of ubiquitin moieties to substrate proteins for degradation via 26S proteasome. However, the known ubiquitin-dependent processes are limited, and the precise regulation of stress-related transcription factors remains to be fully understood. This review outlines the mechanism of E3 ligase-dependent transcription factor degradation and discusses their role in phytohormone signaling.