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

2014; Nature Portfolio; Volume: 5; Issue: 1 Linguagem: Inglês

10.1038/ncomms5687

2041-1723

Mamoona Khan, Wilfried Rozhon, Simon Josef Unterholzner, Tingting Chen, Marina Eremina, Bernhard Wurzinger, Andreas Bachmair, Markus Teige, Tobias Sieberer, Erika Isono, Brigitte Poppenberger,

14-3-3 protein interactions

Brassinosteroids (BRs) are steroid hormones that are essential for plant growth. Responses to these hormones are mediated by transcription factors of the bri1-EMS suppressor 1/brassinazole resistant 1 subfamily, and BRs activate these factors by impairing their inhibitory phosphorylation by GSK3/shaggy-like kinases. Here we show that BRs induce nuclear compartmentalization of CESTA (CES), a basic helix-loop-helix transcription factor that regulates BR 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 BR-deficient situation, CES is phosphorylated to activate target gene transcription and enable further posttranslational modification that controls CES protein stability and nuclear dynamics. Brassinosteroid hormones control plant growth by regulating phosphorylation of a family of transcription factors. Here Khan et al.find that the stability and nuclear localization of the brassinosteroid-sensitive transcription factor CESTA is regulated by antagonistic SUMOylation and phosphorylation.