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

Mamoona Khan, Wilfried Rozhon, Simon Josef Unterholzner, Tingting Chen, Marina Eremina, Bernhard Wurzinger, Andreas Bachmair, Markus Teige, Tobias Sieberer, Erika Isono and Brigitte Poppenberger ()
Additional contact information
Mamoona Khan: Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München
Wilfried Rozhon: Biotechnology of Horticultural Crops, TUM School of Life Sciences Weihenstephan, Technische Universität München
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

Nature Communications, 2014, vol. 5, issue 1, 1-10

Abstract: 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.

Date: 2014
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms5687 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5687

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms5687

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().