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

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  • Mamoona Khan

    (Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München
    Max F. Perutz Laboratories, University of Vienna)

  • Wilfried Rozhon

    (Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München
    Max F. Perutz Laboratories, University of Vienna)

  • Simon Josef Unterholzner

    (Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München)

  • Tingting Chen

    (Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München)

  • Marina Eremina

    (Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München)

  • Bernhard Wurzinger

    (University of Vienna)

  • Andreas Bachmair

    (Max F. Perutz Laboratories, University of Vienna)

  • Markus Teige

    (University of Vienna)

  • Tobias Sieberer

    (Plant Growth Regulation, TUM School of Life Sciences Weihenstephan, Technische Universität München)

  • Erika Isono

    (Plant Systems Biology, TUM School of Life Sciences Weihenstephan, Technische Universität München)

  • Brigitte Poppenberger

    (Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München
    Max F. Perutz Laboratories, University of Vienna)

Abstract

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.

Suggested Citation

  • Mamoona Khan & Wilfried Rozhon & Simon Josef Unterholzner & Tingting Chen & Marina Eremina & Bernhard Wurzinger & Andreas Bachmair & Markus Teige & Tobias Sieberer & Erika Isono & Brigitte Poppenberge, 2014. "Interplay between phosphorylation and SUMOylation events determines CESTA protein fate in brassinosteroid signalling," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5687
    DOI: 10.1038/ncomms5687
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