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

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作者
Mamoona Khan
Wilfried Rozhon
Simon Josef Unterholzner
Tingting Chen
Marina Eremina
Bernhard Wurzinger
Andreas Bachmair
Markus Teige
Tobias Sieberer
Erika Isono
Brigitte Poppenberger
机构
[1] Biotechnology of Horticultural Crops,Department of Molecular Systems Biology
[2] TUM School of Life Sciences Weihenstephan,undefined
[3] Technische Universität München,undefined
[4] Max F. Perutz Laboratories,undefined
[5] University of Vienna,undefined
[6] University of Vienna,undefined
[7] Plant Growth Regulation,undefined
[8] TUM School of Life Sciences Weihenstephan,undefined
[9] Technische Universität München,undefined
[10] Plant Systems Biology,undefined
[11] TUM School of Life Sciences Weihenstephan,undefined
[12] Technische Universität München,undefined
来源
Nature Communications | / 5卷
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摘要
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.
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