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Significance Phosphorylation is essential for the regulation and degradation of PHYTOCHROME-INTERACTING FACTORs (PIFs), key repressors of photomorphogenesis. Although the kinases responsible for PIF phosphorylation have been extensively studied, the phosphatases that dephosphorylate PIFs are largely unknown. Here, we reveal that mutations of FyPP1 and FyPP3, 2 catalytic subunits of PP6 phosphatases, promote seedling photomorphogenesis in the dark. FyPP1 and FyPP3 directly interact with and dephosphorylate PIF3 and PIF4, which may increase the activity of these proteins in the dark and stabilize PIF4 during the dark-to-light transition. The phosphatases identified in this study add a building block to the light signaling network.

Arabidopsis PP6 phosphatases dephosphorylate PIF proteins to repress photomorphogenesis