Ubiquitination in NB-LRR-mediated immunity

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.

► Stability of NB-LRR proteins is controlled by ubiquitination-mediated protein degradation.
► SCFCPR1 targets SNC1 and RPS2 for degradation.
► SRFR1 associates with SGT1 to regulate the stability of NB-LRR proteins.
► R protein stability control prevents auto-immunity caused by over-accumulation of R proteins.
► Regulation of NB-LRR stability by environmental conditions, such as light.
► Roles of E1 and DUBs in the regulation of plant immunity.