Abstract
Small ubiquitin-like modifier (SUMO) post-translational modification (SUMOylation) plays essential roles in regulating various biological processes; however, its function and regulation in the plant light signaling pathway are largely unknown. SEUSS (SEU) is a transcriptional co-regulator that integrates light and temperature signaling pathways, thereby regulating plant growth and development in Arabidopsis thaliana. Here, we show that SEU is a substrate of SUMO1, and that substitution of four conserved lysine residues disrupts the SUMOylation of SEU, impairs its function in photo- and thermomorphogenesis, and enhances its interaction with PHYTOCHROME-INTERACTING FACTOR 4 transcription factors. Furthermore, the SUMO E3 ligase SIZ1 interacts with SEU and regulates its SUMOylation. Moreover, SEU directly interacts with phytochrome B photoreceptors, and the SUMOylation and stability of SEU are activated by light. Our study reveals a novel post-translational modification mechanism of SEU in which light regulates plant growth and development through SUMOylation-mediated protein stability.