ArticleThe Plant cell2026
Phosphorylation of the plant photoreceptor UVR8 regulates its dimer/monomer status and enhances UV-B signaling across species.
Article in The Plant cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Ultraviolet-B (UV-B) is an integral component of sunlight that profoundly shapes plant growth, development, and survival. Plant photoreceptor UV RESISTANCE LOCUS 8 (UVR8) homodimers perceive UV-B and dissociate into active monomers to initiate signaling, yet how UVR8 dimer stability and monomer activity are post-translationally regulated remains unclear. We identify UV-B-enhanced phosphorylation at threonine 356 of UVR8, which promotes UV-B-induced UVR8 dimer dissociation and delays redimerization, shifting dimer/monomer equilibrium towards active monomer in Arabidopsis. Importantly, the same regulatory mechanism is conserved in tomato, demonstrating that phosphorylation at this site represents a broadly applicable molecular switch across species. Moreover, this modification enhances the binding of UVR8 to CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1), prolongs UVR8 nuclear residence, and amplifies UV-B signaling outputs. Together, these findings uncover phosphorylation at T356 as an evolutionarily conserved molecular switch that fine-tunes photoreceptor conformational change and signaling, highlighting phosphorylation as a critical posttranslational control of light perception in plants.
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