The ubiquitin-proteasome system as a transcriptional regulator of plant immunity

Abstract

The ubiquitin-proteasome system (UPS) has been shown to play vital roles in diverse plant developmental and stress responses. The UPS post-translationally modifies cellular proteins with the small molecule ubiquitin, resulting in their regulated degradation by the proteasome. Of particular importance is the role of the UPS in regulating hormone-responsive gene expression profiles, including those triggered by the immune hormone salicylic acid (SA). SA utilizes components of the UPS pathway to reprogram the transcriptome for establishment of local and systemic immunity. Emerging evidence has shown that SA induces the activity of Cullin-RING ligases (CRLs) that fuse chains of ubiquitin to downstream transcriptional regulators and consequently target them for degradation by the proteasome. Here we review how CRL-mediated degradation of transcriptional regulators may control SA-responsive immune gene expression programmes and discuss how the UPS can be modulated by both endogenous and foreign exogenous signals. The highlighted research findings paint a clear picture of the UPS as a central hub for immune activation as well as a battle ground for hijacking by pathogens.