Calmodulin-like protein condensates decode PAMP-induced nuclear calcium to activate plant immunity.

Calcium signatures are key responses to diverse environmental stresses, yet how distinct calcium signals within confined subcellular compartments are decoded remains poorly understood. Calmodulin proteins, serving as canonical calcium sensors, play a vital role in downstream signaling. Notably, plants uniquely possess calmodulin-like (CML) proteins that contain EF-hand motifs and may function as specialized calcium sensors. Here, we find that CML49 and CML50, both of which contain EF-hands and intrinsically disordered regions (IDRs), contribute to pathogen resistance by forming molecular condensates. Pathogen-associated molecular pattern (PAMP) perception induces nuclear calcium signals that promote CML49 and CML50 condensate formation in an EF-hand- and IDR-dependent manner. These condensates sequester the WRKY11/17 transcription factors, thereby suppressing their immune-inhibitory activity. Our findings indicate that CML49/50-mediated condensate assembly spatially silences negative regulators and provides a mechanism for decoding nuclear calcium dynamics to activate plant immune responses.