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Floral transition is influenced by photoperiod and ambient temperature, which are integrated to modulate development via a molecular mechanism that remains to be elucidated. Here we demonstrate that the F-box protein FLAVIN-BINDING, KELCH REPEAT, F-BOX 1 (FKF1) and its interacting partner GIGANTEA (GI), central regulators of photoperiodic flowering, target SHORT VEGETATIVE PHASE (SVP) for 26S-proteasome-dependent degradation to regulate the temperature-responsive developmental transition to flowering. At low temperatures, GI is sequestered in liquid-like nuclear condensates. By contrast, FKF1 accumulates at high temperatures and releases GI from condensates to form a nuclear-dispersed FKF1–GI complex, leading to SVP degradation under short-day conditions. Temperature sensitivity is significantly reduced in fkf1-t, gi-2 and fkf1-2 gi-2 mutants. We propose that the FKF1–GI complex mediates the proteolysis of a floral repressor via reversible liquid–liquid phase separation to accelerate floral transition at high temperatures. © The Author(s), under exclusive licence to Springer Nature Limited 2025.
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