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Article Dans Une Revue Nature Communications Année : 2015

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

Sara Martins
Esther M. N. Dohmann
  • Fonction : Auteur
Anne Cayrel
Alexander Johnson
Wolfgang Fischer
  • Fonction : Auteur
Florence Pojer
  • Fonction : Auteur
Yvon Jaillais
Joanne Chory
  • Fonction : Auteur
Niko Geldner

Résumé

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.

Dates et versions

hal-02397584 , version 1 (06-12-2019)

Identifiants

Citer

Sara Martins, Esther M. N. Dohmann, Anne Cayrel, Alexander Johnson, Wolfgang Fischer, et al.. Internalization and vacuolar targeting of the brassinosteroid hormone receptor BRI1 are regulated by ubiquitination. Nature Communications, 2015, 6, pp.6151. ⟨10.1038/ncomms7151⟩. ⟨hal-02397584⟩
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