A Thermosensor Fust1 Primes Heatinduced Stress Granule Formation Via Biomolecular Condensation In Arabidopsis Pan Geng Changxuan Li Xuebo Quan Jiaxuan Peng Zhiying Yao Yunhe Wang Ming Yang Yanning Wang Yunfan Jin Yan Xiong Hongtao Liu Yijun Qi Peiguo Yang Kai Huang Xiaofeng Fang by Pan Geng & Changxuan Li & Xuebo Quan & Jiaxuan Peng & Zhiying Yao & Yunhe Wang & Ming Yang & Yanning Wang & Yunfan Jin & Yan Xiong & Hongtao Liu & Yijun Qi & Peiguo Yang & Kai Huang & Xiaofeng Fang instant download after payment.

The ability to sense cellular temperature and induce physiological changes is pivotal for plants to cope with warming climate.Biomolecular condensation is emerging as a thermo-sensing mechanism, but the underlying molecular basis remains elusive. Herewe show that an intrinsically disordered protein FUST1 senses heat via its condensation in Arabidopsis thaliana. Heat-dependentcondensation of FUST1 is primarily determined by its prion-like domain (PrLD). All-atom molecular dynamics simulation andexperimental validation reveal that PrLD encodes a thermo-switch, experiencing lock-to-open conformational changes that controlthe intermolecular contacts. FUST1 interacts with integral stress granule (SG) components and localizes in the SGs. Importantly,FUST1 condensation is autonomous and precedes condensation of several known SG markers and is indispensable for SG assembly.1234567890();,:Loss of FUST1 significantly delays SG assembly and impairs both basal and acquired heat tolerance. These findings illuminate themolecular basis for thermo-sensing by biomolecular condensation and shed light on the molecular mechanism of heat stressgranule assembly.Cell Research (2025) 0:1–14;