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Nat Commun. 2015 Jan 21;6:6151. doi: 10.1038/ncomms7151.

Internalization and vacuolar targeting of the brassinosteroid hormone receptor BRI1 are regulated by ubiquitination.

Author information

1
1] Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Paris-Sud University, Avenue de la Terrasse, 91190 Gif-sur-Yvette, France [2] Institut des Sciences du Végétal, Unité Propre de Recherche 2355, Centre National de la Recherche Scientifique, Saclay Plant Sciences, Avenue de la Terrasse, 91190 Gif-sur-Yvette, France.
2
Department of Plant Molecular Biology, University of Lausanne, UNIL-Sorge, 1015 Lausanne, Switzerland.
3
The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.
4
Protein Crystallography Core Facility, Ecole Polytechnique Fédérale de Lausanne, SV 3827 Station 19, 1015 Lausanne, Switzerland.
5
Laboratoire de Reproduction et Développement des Plantes, INRA, CNRS, ENS Lyon, Université de Lyon, 46 allée d'Italie, 69364 Lyon 07, France.
6
1] The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA [2] Howard Hughes Medical Institute, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, California 92037, USA.

Abstract

Brassinosteroids are plant steroid hormones that control many aspects of plant growth and development, and are perceived at the cell surface by the plasma membrane-localized receptor kinase BRI1. Here we show that BRI1 is post-translationally modified by K63 polyubiquitin chains in vivo. Using both artificial ubiquitination of BRI1 and generation of an ubiquitination-defective BRI1 mutant form, we demonstrate that ubiquitination promotes BRI1 internalization from the cell surface and is essential for its recognition at the trans-Golgi network/early endosomes (TGN/EE) for vacuolar targeting. Finally, we demonstrate that the control of BRI1 protein dynamics by ubiquitination is an important control mechanism for brassinosteroid responses in plants. Altogether, our results identify ubiquitination and K63-linked polyubiquitin chain formation as a dual targeting signal for BRI1 internalization and sorting along the endocytic pathway, and highlight its role in hormonally controlled plant development.

PMID:
25608221
PMCID:
PMC4713032
DOI:
10.1038/ncomms7151
[Indexed for MEDLINE]
Free PMC Article

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