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INRA
24, chemin de Borde Rouge –Auzeville – CS52627
31326 Castanet Tolosan CEDEX - France

Dernière mise à jour : Mai 2018

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SPS - Saclay Plant Sciences

Ubiquitin-dependent endocytosis of cell-surface proteins (BRIubi)

Coordinator: Grégory Vert

PhD project selected in 2012 – Person recruited: Sara Carneiro Martins

In plants, the existence of ubiquitin(Ub)-dependent trafficking of plasma membrane proteins has long been undocumented, and the precise mechanisms underlying Ub-mediated dynamics and the identity of factors involved is still elusive. We investigated the roles and the mechanisms of Ub-dependent trafficking of cell-surface membrane proteins, using the brassinosteroid (BR) hormone receptor BRI1. BRI1 indeed represents one of the few plant endocytic substrates, and serves as the archetypal receptor kinase in plants for which the ligand, the activation mechanism, the partners and the downstream signaling pathways are well characterized.  We demonstarted 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 uncovered 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 demonstrated that the control of BRI1 protein dynamics by ubiquitination is an important control mechanism for brassinosteroid responses in plants. Altogether, our results established ubiquitination and K63-linked polyubiquitin chain formation as a dual targeting signal for BRI1 internalization and sorting along the endocytic pathway, and highlighted its role in hormonally controlled plant development.

Publications:

Martins S., Dohmann E.M., Cayrel A., Johnson A., Fischer W., Pojer F., Satiat-Jeunemaitre B., Jaillais Y., Chory J., Geldner N., Vert G. (2015). Internalization and vacuolar targeting of the brassinosteroid hormone receptor BRI1 are regulated by ubiquitination. Nature Communications 6: 6151.

Communications in conferences:

- EPSR 2015 Paris : “Ubiquitin-dependent endocytosis of the plant steroid hormone receptor BRI1”

- Poster at Signalling in Plant Development EMBO Conference in Brno - "Ubiquitin-dependent endocytosis of cell-surface proteins”