Histone deacetylase 9 modulates the acetylation dynamics of phototropin 1 to fine-tune phototropic responses in plants.

ABSTRACT: Phototropism is essential for optimizing plant growth and development, with the blue light receptor phototropin 1 (phot1) acting as the primary photoreceptor. Although downstream components of phot1-mediated phototropic signaling have been studied extensively, the upstream regulatory mechanisms that control phot1 activity remain to be clarified. Here, we demonstrate that lysine acetylation dynamically modifies phot1 under both dark and light conditions. Site-directed mutagenesis of acetylated lysines revealed that acetylation regulates the light-induced autophosphorylation and kinase activity of phot1. Genetic screening of histone deacetylase (HDAC) mutants identified HDA9 as a key regulator of phototropism that physically interacts with phot1, modulating its acetylation and phosphorylatio

SUBMITTER: Liang M 

PROVIDER: S-EPMC12365830 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature