Figure 7
A proposed model for OsPUB15 to regulate PID2-mediated signaling. The unknown ligand from pathogen is likely able to activate the immune receptor PID2 by changing its conformation, which leads directly to the homodimerization and autophosphorylation of PID2. Such phosphorylated form of PID2 then recruits and transphosphorylates OsPUB15. The phosphorylated OsPUB15 serves as an active E3 ligase to mediate the degradation of unknown substrate(s), which is/are likely involved in PID2-mediated immune responses.