Ubiquitination is an essential posttranslational modification and plays a crucial role in regulating plant immunity by modulating protein activity, stability, abundance and interaction. Recently, major breakthroughs have been made in understanding the mechanisms associated with the regulation of immune signaling by ubiquitination. In this mini review, we highlight the recent advances in the role of ubiquitination in fine-tuning the resistance activated by plant pattern recognition receptors (PRRs) and intracellular nucleotide-binding site and leucine-rich repeat domain receptors (NLRs). We also discuss current understanding of the positive regulation of plant immunity by ubiquitination, including the modification of immune negative regulators and of the guardee proteins monitored by NLRs.
Keywords: E3 ubiquitin ligase; Fine-tuning; NLRs; PRRs; Plant immunity; Ubiquitination.
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