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<p>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 <i>fkf1-t</i>, <i>gi-2</i> and <i>fkf1-2</i> <i>gi-2</i> 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.</p>

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High-temperature-induced FKF1 accumulation promotes flowering through the dispersion of GI and degradation of SVP

  • 期刊论文

  • 发表日期：

    2025年7月4日

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  • Hong Gil Lee,
  • Jinkwang Kim,
  • Kyung-Ho Park,
  • Hongwoo Lee,
  • Sol-Bi Kim,
  • Ji-Yul Jung,
  • Eunha Gwak,
  • Ji Hoon Ahn,
  • Jae-Hoon Jung,
  • Jong-Chan Lee,
  • Pil Joon Seo

摘要

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.