SUMMARY
Programmed cell death (PCD) plays critical roles in plant immunity but
must be regulated to prevent excessive damage. The E3 ubiquitin ligase SPL11
negatively regulates PCD and immunity in plants. We show that SPL11
cell-death suppressor 2 (SDS2), an
S-domain receptor-like kinase, positively regulates PCD and immunity in rice by
engaging and regulating SPL11 and related kinases controlling defense responses.
An sds2 mutant shows reduced immune responses and enhanced
susceptibility to the blast fungus Magnaporthe oryzae.
Conversely, SDS2 over-expression induces constitutive PCD
accompanied by elevated immune responses and enhanced resistance to M.
oryzae. SDS2 interacts with and phosphorylates SPL11, which in turn
ubiquitinates SDS2, leading to its degradation. In addition, SDS2 interacts with
related receptor-like cytoplasmic kinases, OsRLCK118/176, that positively
regulate immunity by phosphorylating the NADPH oxidase OsRbohB to stimulate ROS
production. Thus, a plasma membrane-resident protein complex consisting of SDS2,
SPL11, and OsRLCK118/176 controls PCD and immunity in rice.