Interplay between phosphorylation and SUMOylation events determines CESTA protein fate in brassinosteroid signaling

Brassinosteroids are steroid hormones that are essential for plant growth. Responses to these hormones are mediated by transcription factors of the BES1/BZR1 subfamily, and brassinosteroids activate these factors by impairing their inhibitory phosphorylation by GSK3/shaggy-like kinases. Here we show that brassinosteroids induce nuclear compartmentalization of CESTA (CES), a bHLH transcription factor that regulates brassinosteroid responses, and reveal that this process is regulated by CES SUMOylation. We demonstrate that CES contains an extended SUMOylation motif, and that SUMOylation of this motif is antagonized by phosphorylation to control CES subnuclear localization. Moreover, we provide evidence that phosphorylation regulates CES transcriptional activity and protein turnover by the proteasome. A coordinated modification model is proposed in which, in a brassinosteroid-deficient situation, CES is phosphorylated to activate target gene transcription and enable further posttranslational modification that controls CES protein stability.