Bacterial XopR subverts RIN4 complex-mediated plant immunity via plasma membrane-associated percolation

Phytobacteria release type 3 effectors (T3Es) abundant in intrinsically disordered regions (IDRs) to undermine plant defenses. How flexible IDRs contribute to T3Es' function in subverting plant immunity remains unclear. Here, we identify a plant plasma membrane (PM)-associated macromolecular condensation mechanism that governs the sophisticated interplay between T3E XopR and the plant's Resistance to Pseudomonas syringae pv. maculicola 1 (RPM1)-interacting protein 4 (RIN4) immune complex. Upon deployment into plants, XopR undergoes PM association, percolation clustering, and spanning networking on the PM, ranging from subnanomolar to tens of nanomolar. This spatiotemporal building of the XopR network enables an efficient manipulation of plant surface immune regulators, including a coiled-coil nucleotide-binding leucine-rich repeat receptor (CNL)-guardee complex with highly disordered RIN4. When XopR hijacks and fluidizes the RIN4-RPM1 condensates, Arabidopsis shows reduced RIN4 phosphorylation and diminished RPM1-activated defense in vivo, consistent with XopR-impaired RIN4 phosphorylation by RPM1-interacting protein kinase (RIPK). Our research illuminates the mechanism underlying the dynamic interplay between bacterial T3Es and plant receptor complex condensates during infection.