In plants, pathogen effector-triggered immunity (ETI) often leads to programmed cell death, which is restricted by NPR1, an activator of systemic acquired resistance. However, the biochemical activities of NPR1 enabling it to promote defense and restrict cell death remain unclear. Here we show that NPR1 promotes cell survival by targeting substrates for ubiquitination and degradation through formation of salicylic acid-induced NPR1 condensates (SINCs). SINCs are enriched with stress response proteins, including nucleotide-binding leucine-rich repeat immune receptors, oxidative and DNA damage response proteins, and protein quality control machineries. Transition of NPR1 into condensates is required for formation of the NPR1-Cullin 3 E3 ligase complex to ubiquitinate SINC-localized substrates, such as EDS1 and specific WRKY transcription factors, and promote cell survival during ETI. Our analysis of SINCs suggests that NPR1 is centrally integrated into the cell death or survival decisions in plant immunity by modulating multiple stress-responsive processes in this quasi-organelle. Display omitted •NPR1 promotes ubiquitination of cytoplasmic proteins upon SA induction•SA-induced NPR1 condensates (SINCs) in cytoplasm are enriched with stress proteins•SINC induction facilitates formation of the NPR1-Cullin 3 E3 ubiquitin ligase complex•SINC is a hub in promoting plant cell survival against biotic and abiotic stresses The immune regulator NPR1 promotes defense and restricts cell death by forming condensates that target specific substrates for degradation in response to salicylic acid signaling.