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

Sara Martins, Esther M. N. Dohmann, Anne Cayrel, Alexander Johnson, Wolfgang Fischer, Florence Pojer, Béatrice Satiat-Jeunemaître, Yvon Jaillais, Joanne Chory, Niko Geldner and Grégory Vert ()
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Sara Martins: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Paris-Sud University
Esther M. N. Dohmann: University of Lausanne
Anne Cayrel: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Paris-Sud University
Alexander Johnson: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Paris-Sud University
Wolfgang Fischer: The Salk Institute for Biological Studies
Florence Pojer: Protein Crystallography Core Facility, Ecole Polytechnique Fédérale de Lausanne
Béatrice Satiat-Jeunemaître: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Paris-Sud University
Yvon Jaillais: Laboratoire de Reproduction et Développement des Plantes, INRA, CNRS, ENS Lyon, Université de Lyon
Joanne Chory: The Salk Institute for Biological Studies
Niko Geldner: University of Lausanne
Grégory Vert: Institute for Integrative Biology of the Cell (I2BC), CNRS, CEA, Paris-Sud University

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms7151

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