As a common protein modification, ubiquitination is used for regulating the fate of protein targets, notably in terms of stability. In recent years, it has emerged to play key roles in the regulation of plant defense responses. Given its flexibility and critical roles in signaling, primarily in the control of protein turnover, ubiquitination is probably targeting many major immune regulators for modification or degradation. In this review, we summarize the latest findings on how different components of the ubiquitination pathway are involved in NB-LRR R protein-mediated immunity.
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