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14 results on '"Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET)"'

1. Getting to the root of plant iron uptake and cell-cell transport: Polarity matters!

Author

Enric Zelazny, Guillaume Dubeaux, Grégory Vert, Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes ( UBINET ), Département Biologie Cellulaire ( BioCell ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Sud - Paris 11 ( UP11 ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Sud - Paris 11 ( UP11 ) -Institut de Biologie Intégrative de la Cellule ( I2BC ), and Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Sud - Paris 11 ( UP11 ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Sud - Paris 11 ( UP11 )

Subjects
0106 biological sciences, Cell type, Polarity (physics), [SDV]Life Sciences [q-bio], Endocytic cycle, Cell, metals, plant nutrition, Biology, Endocytosis, 01 natural sciences, 03 medical and health sciences, iron, medicine, endocytosis, polarity, Vascular tissue, 030304 developmental biology, 0303 health sciences, [ SDV ] Life Sciences [q-bio], Transporter, Cell biology, Article Addendum, medicine.anatomical_structure, Membrane protein, General Agricultural and Biological Sciences, 010606 plant biology & botany
Abstract

International audience; Plasma membrane proteins play pivotal roles in mediating responses to endogenous and environmental cues. Regulation of membrane protein levels and establishment of polarity are fundamental for many cellular processes. In plants, IRON-REGULATED TRANSPORTER 1 (IRT1) is the major root iron transporter but is also responsible for the absorption of other divalent metals such as manganese, zinc and cobalt. We recently uncovered that IRT1 is polarly localized to the outer plasma membrane domain of plant root epidermal cells upon depletion of its secondary metal substrates. The endosome-recruited FYVE1 protein interacts with IRT1 in the endocytic pathway and plays a crucial role in the establishment of IRT1 polarity, likely through its recycling to the cell surface. Our work sheds light on the mechanisms of radial transport of nutrients across the different cell types of plant roots toward the vascular tissues and raises interesting parallel with iron transport in mammals.

Published
2015
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2. Brassinosteroid signaling and BRI1 dynamics went underground

Author

Grégory Vert, Yvon Jaillais, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), European Research Council [3363360-APPL], Marie Curie Action [PCIG-GA-2011-303601, PCIG-GA-2012-334021], Agence Nationale de la Recherche [ANR-13-JSV2-0004-01], Kimberley C Snowden, and Dirk Inze

Subjects
0301 basic medicine, [SDV]Life Sciences [q-bio], Meristem, Cell, Arabidopsis, Context (language use), Plant Science, Plant Roots, Article, Cell membrane, 03 medical and health sciences, chemistry.chemical_compound, Plant Growth Regulators, Brassinosteroids, Botany, medicine, Brassinosteroid, biology, Arabidopsis Proteins, fungi, biology.organism_classification, Cell biology, 030104 developmental biology, medicine.anatomical_structure, chemistry, Signal transduction, Protein Kinases, Signal Transduction, Hormone
Abstract

Brassinosteroids (BRs) are a group of steroid molecules perceived at the cell surface and that act as plant hormones. Since their discovery as crucial growth substances, BRs were mainly studied for their action in above ground organs and the BR signaling pathway was largely uncovered in the context of hypocotyl elongation. However, for the past two years, most of the exciting findings on BR signaling have been made using roots as a model. The Arabidopsis root is a system of choice for cell biology and allowed detailed characterization of BR perception at the cell membrane. In addition, a series of elegant articles dissected how BRs act in tissue specific manners to control root growth and development.

Published
2016
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3. Metal Sensing by the IRT1 Transporter-Receptor Orchestrates Its Own Degradation and Plant Metal Nutrition

Author

Enric Zelazny, Grégory Vert, Julie Neveu, Guillaume Dubeaux, Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut de génétique et microbiologie [Orsay] (IGM), and Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0106 biological sciences, 0301 basic medicine, Transcription, Genetic, [SDV]Life Sciences [q-bio], Arabidopsis, plant, Vacuole, Plant Roots, 01 natural sciences, transceptor, Gene Expression Regulation, Plant, Cation Transport Proteins, sensing, degradation, 2. Zero hunger, Cadmium, biology, Protein Stability, phosphorylation, Intracellular Signaling Peptides and Proteins, Plants, Genetically Modified, Endocytosis, Ubiquitin ligase, Protein Transport, Metals, visual_art, transporter, visual_art.visual_art_medium, Phosphorylation, Receptor, Endosome, chemistry.chemical_element, Saccharomyces cerevisiae, Protein Serine-Threonine Kinases, Metal, 03 medical and health sciences, ubiquitin, Molecular Biology, Arabidopsis Proteins, Ubiquitination, Biological Transport, Transporter, Cell Biology, 030104 developmental biology, chemistry, Proteolysis, Vacuoles, biology.protein, Biophysics, metal homeostasis, Carrier Proteins, 010606 plant biology & botany
Abstract

Plant roots forage the soil for iron, the concentration of which can be dramatically lower than those needed for growth. Soil iron uptake uses the broad metal spectrum IRT1 transporter that also transports zinc, manganese, cobalt, and cadmium. Sophisticated iron-dependent transcriptional regulatory mechanisms allow plants to tightly control the abundance of IRT1, ensuring optimal absorption of iron. Here, we uncover that IRT1 acts as a transporter and receptor (transceptor), directly sensing excess of its non-iron metal substrates in the cytoplasm, to regulate its own degradation. Direct metal binding to a histidine-rich stretch in IRT1 triggers its phosphorylation by the CIPK23 kinase and facilitates the subsequent recruitment of the IDF1 E3 ligase. CIPK23-driven phosphorylation and IDF1-mediated lysine-63 polyubiquitination are jointly required for efficient endosomal sorting and vacuolar degradation of IRT1. Thus, IRT1 directly senses elevated non-iron metal concentrations and integrates multiple substrate-dependent regulations to optimize iron uptake and protect plants from highly reactive metals.

Published
2018
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4. Nonselective Chemical Inhibition of Sec7 Domain-Containing ARF GTPase Exchange Factors

Author

Steven De Munck, Riet De Rycke, Bram Denoo, Sacco C. de Vries, Jan Hullaert, Wim Annaert, Isha Sharma, Kaija Goodman, Wim Dejonghe, Johan M. Winne, Marisa S. Otegui, François Peurois, Wim Nerinckx, Andrzej Drozdzecki, Annemieke Madder, Jacqueline Cherfils, Marine Bretou, Qing Lu, Sara Martins, Sjef Boeren, Grégory Vert, Kamila Kalinowska, Veronique Storme, Long Nguyen, Dominique Audenaert, Erika Isono, Kiril Mishev, Savvas N. Savvides, Eugenia Russinova, Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS), Department of Plant Systems Biology, Flanders Institute for Biotechnology, Ghent University Hospital, Laboratory of Biochemistry, Wageningen University and Research [Wageningen] (WUR), Immunité et cancer (U932), Université Paris Descartes - Paris 5 (UPD5)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratory for Protein Biochemistry and Biomolecular Engineering, Department of Biochemistry, Physiology and Microbiology, Universiteit Gent = Ghent University [Belgium] (UGENT), Department of Plant Biotechnology and Bioinformatics, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Ghent University, Compound Screening Facility, VIB, Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Organic and Biomimetic Chemistry Research Group, VIB-UGent Center for Inflammation Research [Gand, Belgique] (IRC), VIB [Belgium], Laboratory for Protein Biochemistry and Biomolecular Engineering, Department of Biochemistry and Microbiology, Laboratory of Membrane Trafficking and VIB11, Center for Human Genetics, Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Polymer Research Group, State Univ Ghent, Department of Systems Biology, Institut d’Électronique, de Microélectronique et de Nanotechnologie (IEMN) - UMR 8520 (IEMN), Ecole Centrale de Lille-Institut supérieur de l'électronique et du numérique (ISEN)-Université de Valenciennes et du Hainaut-Cambrésis (UVHC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Université Polytechnique Hauts-de-France (UPHF), Ghent University [Belgium] (UGENT), Laboratoire de dynamique membranaire et maladies neurologiques (UMR 8192), Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), VIB Inflammation Research Center, Laboratoire d'enzymologie et biochimie structurales (LEBS), Centre National de la Recherche Scientifique (CNRS), Universiteit Gent = Ghent University (UGENT), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Curie [Paris]-Université Paris Descartes - Paris 5 (UPD5), Universiteit Gent [Ghent], Centre National de la Recherche Scientifique (CNRS)-Université de Lille-Université Polytechnique Hauts-de-France (UPHF)-Ecole Centrale de Lille-Université Polytechnique Hauts-de-France (UPHF)-Institut supérieur de l'électronique et du numérique (ISEN), Wageningen University and Research Centre [Wageningen] (WUR), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Université Paris Descartes - Paris 5 (UPD5)-Institut Curie-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), and Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, ADP ribosylation factor, Endosome, [SDV]Life Sciences [q-bio], Arabidopsis, Biochemie, Endosomes, Plant Science, arabidopsis-thaliana, Biology, receptor kinase bri1, Endocytosis, Biochemistry, UBINET, Piperazines, 03 medical and health sciences, symbols.namesake, chemistry.chemical_compound, golgi network/early endosome, BIOCELL, Guanine Nucleotide Exchange Factors, Life Science, Endomembrane system, endomembrane trafficking, Research Articles, brefeldin-a, Brefeldin A, protein complexes, Arabidopsis Proteins, plasma-membrane, plant-cells, Cell Biology, Golgi apparatus, Plants, Genetically Modified, Transport protein, Cell biology, wide analysis, Protein Transport, small molecules, 030104 developmental biology, chemistry, Vacuoles, symbols, Phthalazines, Guanine nucleotide exchange factor, Protein Kinases
Abstract

International audience; Small GTP-binding proteins from the ADP-ribosylation factor (ARF) family are important regulators of vesicle formation and cellular trafficking in all eukaryotes. ARF activation is accomplished by a protein family of guanine nucleotide exchange factors (GEFs) that contain a conserved catalytic Sec7 domain. Here, we identified and characterized Secdin, a small-molecule inhibitor of Arabidopsis thaliana ARF-GEFs. Secdin application caused aberrant retention of plasma membrane (PM) proteins in late endosomal compartments, enhanced vacuolar degradation, impaired protein recycling, and delayed secretion and endocytosis. Combined treatments with Secdin and the known ARF-GEF inhibitor Brefeldin A (BFA) prevented the BFA-induced PM stabilization of the ARF-GEF GNOM, impaired its translocation from the Golgi to the trans-Golgi network/early endosomes, and led to the formation of hybrid endomembrane compartments reminiscent of those in ARF-GEF-deficient mutants. Drug affinity-responsive target stability assays revealed that Secdin, unlike BFA, targeted all examined Arabidopsis ARF-GEFs, but that the interaction was probably not mediated by the Sec7 domain because Secdin did not interfere with the Sec7 domain-mediated ARF activation. These results show that Secdin and BFA affect their protein targets through distinct mechanisms, in turn showing the usefulness of Secdin in studies in which ARF-GEF-dependent endomembrane transport cannot be manipulated with BFA.

Published
2018
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5. Mapping of Plasma Membrane Proteins Interacting With Arabidopsis thaliana Flotillin 2

Author

Petra Junková, Michal Daněk, Daniela Kocourková, Jitka Brouzdová, Kristýna Kroumanová, Enric Zelazny, Martin Janda, Radovan Hynek, Jan Martinec, Olga Valentová, Czech Academy of Sciences [Prague] (CAS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institute of Experimental Botany of the Czech Academy of Sciences (IEB / CAS), Institute of Chemical Technology [Prague] (ICT), and University of Chemistry and Technology Prague (UCT Prague)

Subjects
0301 basic medicine, water transport, intracellular trafficking, ATPase, [SDV]Life Sciences [q-bio], plant–pathogen interaction, Aquaporin, Plant Science, protein–protein interactions, lcsh:Plant culture, UBINET, immunopurification, Protein–protein interaction, 03 medical and health sciences, Arabidopsis, BIOCELL, Arabidopsis thaliana, lcsh:SB1-1110, Original Research, mass spectrometry, Water transport, biology, split-ubiquitin yeast system, Chemistry, biology.organism_classification, Cell biology, 030104 developmental biology, Membrane protein, Arabidopsis flotillin 2, biology.protein, Intracellular
Abstract

Arabidopsis flotillin 2 (At5g25260) belongs to the group of plant flotillins, which are not well characterized. In contrast, metazoan flotillins are well known as plasma membrane proteins associated with membrane microdomains that act as a signaling hub. The similarity of plant and metazoan flotillins, whose functions most likely consist of affecting other proteins via protein-protein interactions, determines the necessity of detecting their interacting partners in plants. Nevertheless, identifying the proteins that form complexes on the plasma membrane is a challenging task due to their low abundance and hydrophobic character. Here we present an approach for mapping Arabidopsis thaliana flotillin 2 plasma membrane interactors, based on the immunoaffinity purification of crosslinked and enriched plasma membrane proteins with mass spectrometry detection. Using this approach, 61 proteins were enriched in the AtFlot-GFP plasma membrane fraction, and 19 of them were proposed to be flotillin 2 interaction partners. Among our proposed partners of Flot2, proteins playing a role in the plant response to various biotic and abiotic stresses were detected. Additionally, the use of the split-ubiquitin yeast system helped us to confirm that plasma-membrane ATPase 1, early-responsive to dehydration stress protein 4, syntaxin-71, harpin-induced protein-like 3, hypersensitive-induced response protein 2 and two aquaporin isoforms interact with flotillin 2 directly. Based on the results of our study and the reported properties of Flot2 interactors, we propose that Flot2 complexes may be involved in plant-pathogen interactions, water transport and intracellular trafficking.

Published
2018
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6. Proteasome-independent functions of lysine-63 polyubiquitination in plants

Author

Natali Romero-Barrios, Grégory Vert, Institut des Sciences des Plantes de Paris-Saclay (IPS2 (UMR_9213 / UMR_1403)), Institut National de la Recherche Agronomique (INRA)-Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, and Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay

Subjects
0301 basic medicine, Proteasome Endopeptidase Complex, autophagy, Physiology, [SDV]Life Sciences [q-bio], ved/biology.organism_classification_rank.species, Lysine, Plant Science, UBINET, 03 medical and health sciences, Ubiquitin, Plant Cells, BIOCELL, ubiquitin, endocytosis, Amino Acid Sequence, Model organism, Polyubiquitin, 2. Zero hunger, biology, ved/biology, plants, Autophagy, Protein turnover, Ubiquitination, food and beverages, Plant cell, Cell biology, 030104 developmental biology, Proteasome, post-translational modification, biology.protein, signaling, Function (biology), lysine-63 polyubiquitination
Abstract

Contents Summary 995 I. Introduction 995 II. The plant Ub machinery 996 III. From Ub to Ub linkage types in plants 997 IV. Increasing analytical resolution for K63 polyUb in plants 998 V. How to build K63 polyUb chains? 998 VI. Cellular roles of K63 polyUb in plants 999 VII. Physiological roles of K63 polyUb in plants 1004 VIII. Future perspectives: towards the next level of the Ub code 1006 Acknowledgements 1006 References 1007 SUMMARY: Ubiquitination is a post-translational modification essential for the regulation of eukaryotic proteins, having an impact on protein fate, function, localization or activity. What originally appeared to be a simple system to regulate protein turnover by the 26S proteasome is now known to be the most intricate regulatory process cells have evolved. Ubiquitin can be arranged in countless chain assemblies, triggering various cellular outcomes. Polyubiquitin chains using lysine-63 from ubiquitin represent the second most abundant type of ubiquitin modification. Recent studies have exposed their common function in proteasome-independent functions in non-plant model organisms. The existence of lysine-63 polyubiquitination in plants is, however, only just emerging. In this review, we discuss the recent advances on the characterization of ubiquitin chains and the molecular mechanisms driving the formation of lysine-63-linked ubiquitin modifications. We provide an overview of the roles associated with lysine-63 polyubiquitination in plant cells in the light of what is known in non-plant models. Finally, we review the crucial roles of lysine-63 polyubiquitin-dependent processes in plant growth, development and responses to environmental conditions.

Published
2018
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7. Regulation of Iron Uptake by IRT1: Endocytosis Pulls the Trigger

Author

Enric Zelazny, Grégory Vert, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
0106 biological sciences, [SDV]Life Sciences [q-bio], Iron, Arabidopsis, chemistry.chemical_element, Endosomes, Plant Science, Zinc, Manganese, Biology, Endocytosis, 01 natural sciences, 03 medical and health sciences, Cation Transport Proteins, Molecular Biology, 030304 developmental biology, 0303 health sciences, Cadmium, Arabidopsis Proteins, Ubiquitin, Transporter, Cell biology, chemistry, Biochemistry, Cobalt, Intracellular, Homeostasis, 010606 plant biology & botany
Abstract

The past two decades of research on plant iron nutrition have completed the casting of the major transporters involved in iron uptake from the soil, long-distance transport, and intracellular distribution. Among these transporters, most of the attention was given to the root iron transporter IRT1, which plays a critical role in iron uptake from the soil and mediates transport of other non-iron metals (zinc, manganese, cobalt, cadmium) under iron-limiting conditions. As such, IRT1 is the primary determinant of iron and heavy metal homeostasis in plants.

Published
2015
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8. Probing Activation and Deactivation of the BRASSINOSTEROID INSENSITIVE1 Receptor Kinase by Immunoprecipitation

Author

Yvon Jaillais, Sara Martins, Grégory Vert, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Reproduction et développement des plantes (RDP), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), European Research Council, I2BC - Institut de Biologie Intégrative de la Cellule, and École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
0301 basic medicine, Receptor complex, Immunoprecipitation, [SDV]Life Sciences [q-bio], Blotting, Western, Arabidopsis, Article, Protein–protein interaction, protein-protein interaction, BRI1, 03 medical and health sciences, chemistry.chemical_compound, Ubiquitin, Gene Expression Regulation, Plant, Brassinosteroids, Brassinosteroid, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Phosphorylation, Receptor, biology, Arabidopsis Proteins, Kinase, fungi, Ubiquitination, Plants, Genetically Modified, Enzyme Activation, 030104 developmental biology, Biochemistry, chemistry, Seedlings, brassinosteroid, biology.protein, Protein Kinases, Protein Processing, Post-Translational, Protein Binding, Signal Transduction
Abstract

International audience; Brassinosteroids (BRs) are sterol-derived hormones that control plant growth and development. The BR receptor complex is encoded by the BRASSINOSTEROID INSENSITIVE1 (BRI1) and members of the SOMATIC EMBRYOGENESIS RECEPTOR KINASE family. For activation and deactivation, the BR receptor complex uses different posttranslational modifications and recruits various partner proteins. Here, we describe optimized immunoprecipitation protocols and variants for biochemical analyses of posttranslational modifications of BRI1 and of protein-protein interactions.

Published
2017
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9. Zooming into plant ubiquitin-mediated endocytosis

Author

Guillaume Dubeaux, Grégory Vert, Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Endosome, media_common.quotation_subject, [SDV]Life Sciences [q-bio], Cell, Cellular functions, Plant Science, Endosomes, Endocytosis, UBINET, 03 medical and health sciences, Ubiquitin, BIOCELL, medicine, Internalization, media_common, Plant Proteins, biology, Endosomal Sorting Complexes Required for Transport, Membrane Proteins, food and beverages, Plants, Cell biology, 030104 developmental biology, medicine.anatomical_structure, Membrane protein, biology.protein
Abstract

Endocytosis in plants plays an essential role, not only for basic cellular functions but also for growth, development, and environmental responses. Over the past few years, ubiquitin emerged as a major signal triggering the removal of plasma membrane proteins from the cell surface and promoting their vacuolar targeting. Detailed genetic, biochemical and imaging studies have provided initial insights into the precise mechanisms and roles of ubiquitin-mediated endocytosis in plants. Here, we summarize the present state of knowledge about the machinery involved in plant ubiquitin-mediated endocytosis and how this is coordinated in time and space to control the internalization and the endosomal sorting of endocytosed proteins.

Published
2017
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10. Single Event Resolution of Plant Plasma Membrane Protein Endocytosis by TIRF Microscopy

Author

Johnson, Alexander, Vert, Grégory, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
plants, trafficking, [SDV]Life Sciences [q-bio], Methods, Arabidopsis, endocytosis, lcsh:SB1-1110, Plant Science, lcsh:Plant culture, imaging techniques, TIRF microscopy
Abstract

Endocytosis is a key process in the internalization of extracellular materials and plasma membrane proteins, such as receptors and transporters, thereby controlling many aspects of cell signaling and cellular homeostasis. Endocytosis in plants has an essential role not only for basic cellular functions but also for growth and development, nutrient delivery, toxin avoidance, and pathogen defense. The precise mechanisms of endocytosis in plants remain quite elusive. The lack of direct visualization and examination of single events of endocytosis has greatly hampered our ability to precisely monitor the cell surface lifetime and the recruitment profile of proteins driving endocytosis or endocytosed cargos in plants. Here, we discuss the necessity to systematically implement total internal reflection fluorescence microcopy (TIRF) in the Plant Cell Biology community and present reliable protocols for high spatial and temporal imaging of endocytosis in plants using clathrin-mediated endocytosis as a test case, since it represents the major route for internalization of cell-surface proteins in plants. We developed a robust method to directly visualize cell surface proteins using TIRF microscopy combined to a high throughput, automated and unbiased analysis pipeline to determine the temporal recruitment profile of proteins to single sites of endocytosis, using the departure of clathrin as a physiological reference for scission. Using this 'departure assay', we assessed the recruitment of two different AP-2 subunits, alpha and mu, to the sites of endocytosis and found that AP2A1 was recruited in concert with clathrin, while AP2M was not. This validated approach therefore offers a powerful solution to better characterize the plant endocytic machinery and the dynamics of one's favorite cargo protein.

Published
2017
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11. Brassinosteroid signaling-dependent root responses to prolonged elevated ambient temperature

Author

Martins, Sara, Montiel-Jorda, Alvaro, Cayrel, Anne, Huguet, Stéphanie, Roux, Christine Paysant-Le, Ljung, Karin, Vert, Grégory, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), PhD fellowship from the Saclay Plant Sciences LabEx initiative - French government [ANR-10-LABX-0040-SPS], Agence Nationale de la Recherche [ANR-11-IDEX-0003-02, ANR-13-JSV2-0004-01], Swedish Governmental Agency for Innovation Systems (VINNOVA), Swedish Research Council (VR), Kempestiftelserna, CNRS (ATIP), and Marie Curie Action [PCIG-GA-2012-334021]

Subjects
Microscopy, Confocal, Indoleacetic Acids, Arabidopsis Proteins, Science, Gene Expression Profiling, [SDV]Life Sciences [q-bio], Blotting, Western, fungi, Arabidopsis, Temperature, Gene Expression Regulation, Developmental, food and beverages, Plants, Genetically Modified, Plant Roots, Article, Gene Expression Regulation, Plant, Brassinosteroids, Mutation, Protein Kinases, Plant Shoots, Signal Transduction
Abstract

Due to their sessile nature, plants have to cope with and adjust to their fluctuating environment. Temperature elevation stimulates the growth of Arabidopsis aerial parts. This process is mediated by increased biosynthesis of the growth-promoting hormone auxin. How plant roots respond to elevated ambient temperature is however still elusive. Here we present strong evidence that temperature elevation impinges on brassinosteroid hormone signaling to alter root growth. We show that elevated temperature leads to increased root elongation, independently of auxin or factors known to drive temperature-mediated shoot growth. We further demonstrate that brassinosteroid signaling regulates root responses to elevated ambient temperature. Increased growth temperature specifically impacts on the level of the brassinosteroid receptor BRI1 to downregulate brassinosteroid signaling and mediate root elongation. Our results establish that BRI1 integrates temperature and brassinosteroid signaling to regulate root growth upon long-term changes in environmental conditions associated with global warming., Moderate heat stimulates the growth of Arabidopsis shoots in an auxin-dependent manner. Here, Martins et al. show that elevated ambient temperature modifies root growth by reducing the BRI1 brassinosteroid-receptor protein level and downregulating brassinosteroid signaling.

Published
2017
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12. A versatile Multisite Gateway-compatible promoter and transgenic line collection for cell type-specific functional genomics in Arabidopsis

Author

Yvon Jaillais, Ana Karina Morao, Maria Mar Marquès-Bueno, Grégory Vert, Marie Barberon, Vincent Colot, François Roudier, Erwann Caillieux, Anne Cayrel, Matthieu Pierre Platre, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), European Research Council - ERC [3363360-APPL], Marie Curie Action - CIG Grant Agreement under the European Union's Seventh Framework Programme [PCIG-GA-2011-303601], CNRS, Agence Nationale de la Recherche, French Ministere de la Recherche et de l'Enseignement Superieur, Agence Nationale de la Recherche [ANR-13-JSV2-0004-01], Marie Curie Action under the European Union's Seventh Framework Programme [PCIG12-GA-2012-334021], and European Project: 257082,EC:FP7:HEALTH,FP7-HEALTH-2010-two-stage,EPIGENESYS(2010)

Subjects
0301 basic medicine, Cell type, SAND lines, RED TIDE lines, [SDV]Life Sciences [q-bio], Cell, Arabidopsis, Genetically Modified, Plant Science, Biology, Article, Promoter Regions, 03 medical and health sciences, Genetic, Gene Expression Regulation, Plant, Gene expression, Genetics, medicine, INTACT, BREAK lines, genomics, Promoter Regions, Genetic, Regulation of gene expression, Gene knockdown, Arabidopsis Proteins, Cell Biology, Plant, Plants, Plants, Genetically Modified, biology.organism_classification, Chromatin, Cell biology, 030104 developmental biology, medicine.anatomical_structure, Gene Expression Regulation, LINE UP lines, Functional genomics
Abstract

Multicellular organisms are composed of many cell types that acquire their specific fate through a precisely controlled pattern of gene expression in time and space dictated in part by cell type-specific promoter activity. Understanding the contribution of highly specialized cell types in the development of a whole organism requires the ability to isolate or analyze different cell types separately. We have characterized and validated a large collection of root cell type-specific promoters and have generated cell type-specific marker lines. These benchmarked promoters can be readily used to evaluate cell type-specific complementation of mutant phenotypes, or to knockdown gene expression using targeted expression of artificial miRNA. We also generated vectors and characterized transgenic lines for cell type-specific induction of gene expression and cell type-specific isolation of nuclei for RNA and chromatin profiling. Vectors and seeds from transgenic Arabidopsis plants will be freely available, and will promote rapid progress in cell type-specific functional genomics. We demonstrate the power of this promoter set for analysis of complex biological processes by investigating the contribution of root cell types in the IRT1-dependent root iron uptake. Our findings revealed the complex spatial expression pattern of IRT1 in both root epidermis and phloem companion cells and the requirement for IRT1 to be expressed in both cell types for proper iron homeostasis.

Published
2016
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13. Unraveling K63 Polyubiquitination Networks by Sensor-Based Proteomics

Author

Alexander W. Johnson, Grégory Vert, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
0106 biological sciences, 0301 basic medicine, Proteomics, Saccharomyces cerevisiae Proteins, Physiology, [SDV]Life Sciences [q-bio], Lysine, Arabidopsis, Plant Science, macromolecular substances, Biosensing Techniques, Tandem mass spectrometry, 01 natural sciences, Interactome, environment and public health, 03 medical and health sciences, Ubiquitin, Tandem Mass Spectrometry, Genetics, Arabidopsis thaliana, biology, Endosomal Sorting Complexes Required for Transport, Arabidopsis Proteins, Ubiquitination, Breakthrough Technologies, biology.organism_classification, Plants, Genetically Modified, Cell biology, Transport protein, Protein Transport, 030104 developmental biology, Biochemistry, biology.protein, 010606 plant biology & botany
Abstract

The polybiquitination of proteins can take on different topologies depending on the residue from ubiquitin involved in the chain formation. Although the role of lysine-48 (K48) polyubiquitination in proteasome-mediated degradation is fairly well characterized, much less is understood about the other types of ubiquitin chains and proteasome-independent functions. To overcome this, we developed a K63 polyubiquitin-specific sensor-based approach to track and isolate K63 polyubiquitinated proteins in plants. Proteins carrying K63 polyubiquitin chains were found to be enriched in diverse membrane compartments as well as in nuclear foci. Using liquid chromatography-tandem mass spectrometry, we identified over 100 proteins from Arabidopsis (Arabidopsis thaliana) that are modified with K63 polyubiquitin chains. The K63 ubiquitinome contains critical factors involved in a wide variety of biological processes, including transport, metabolism, protein trafficking, and protein translation. Comparison of the proteins found in this study with previously published nonresolutive ubiquitinomes identified about 70 proteins as ubiquitinated and specifically modified with K63-linked chains. To extend our knowledge about K63 polyubiquitination, we compared the K63 ubiquitinome with K63 ubiquitination networks based on the Arabidopsis interactome. Altogether, this work increases our resolution of the cellular and biological roles associated with this poorly characterized posttranslational modification and provides a unique insight into the networks of K63 polyubiquitination in plants.

Published
2016
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14. Internalization and vacuolar targeting of the brassinosteroid hormone receptor BRI1 are regulated by ubiquitination

Author

Anne Cayrel, Niko Geldner, Wolfgang H. Fischer, Esther M. N. Dohmann, Sara Martins, Béatrice Satiat-Jeunemaitre, Florence Pojer, Alexander W. Johnson, Joanne Chory, Yvon Jaillais, Grégory Vert, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Dynamique de la Compartimentation cellulaire dans les cellules de plantes supérieures (DYNBSJ), Département Biologie Cellulaire (BioCell), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Signalisation Cellulaire et Ubiquitination chez les plantes (UBINET), 'Infrastructures en Biologie Sante et Agronomie' (IBiSA), French National Research Agency under Investments for the Future programmes 'France-BioImaging infrastructure' [ANR-10-INSB-04-01], Saclay Plant Sciences initiative [ANR-10-LABX-0040-SPS], 'Conseil General de l'Essonne', Saclay Plant Sciences LabEx initiative - French government [ANR-10-LABX-0040-SPS], Agence Nationale de la Recherche [ANR-11-IDEX-0003-02, ANR-13-JSV2-0004-01], EMBO long-term fellowship, National Institutes of Health [5 R01 GM094428], Howard Hughes Medical Institute, Swiss National Science Foundation [31003A_120558], and Marie Curie Action [PCIG-GA-2012-334021]

Subjects
0106 biological sciences, [SDV]Life Sciences [q-bio], Endocytic cycle, Arabidopsis, General Physics and Astronomy, 01 natural sciences, UBINET, chemistry.chemical_compound, Ubiquitin, Gene Expression Regulation, Plant, Brassinosteroid, Phosphorylation, Internalization, Receptor, Polyubiquitin, media_common, 0303 health sciences, Microscopy, Multidisciplinary, biology, Atomic and molecular interactions with photons, Plants, Protein-Serine-Threonine Kinases, Plants, Genetically Modified, Cell biology, Transport protein, Protein Transport, Signal transduction, Signal Transduction, trans-Golgi Network, DYNBSJ, Endosome, media_common.quotation_subject, Genetically Modified, Endosomes, Protein Serine-Threonine Kinases, Article, General Biochemistry, Genetics and Molecular Biology, Fluorescence, 03 medical and health sciences, Arabidopsis/genetics, Arabidopsis/metabolism, Arabidopsis Proteins/genetics, Arabidopsis Proteins/metabolism, Brassinosteroids/metabolism, Cell Membrane/metabolism, Cell Membrane/ultrastructure, Endosomes/metabolism, Endosomes/ultrastructure, Lysine/metabolism, Microscopy, Fluorescence/methods, Polyubiquitin/genetics, Polyubiquitin/metabolism, Protein Kinases/genetics, Protein Kinases/metabolism, Protein-Serine-Threonine Kinases/genetics, Protein-Serine-Threonine Kinases/metabolism, Vacuoles/metabolism, Vacuoles/ultrastructure, trans-Golgi Network/metabolism, trans-Golgi Network/ultrastructure, Brassinosteroids, Author Correction, Protein Processing, 030304 developmental biology, Attosecond science, Arabidopsis Proteins, Lysine, fungi, Cell Membrane, Post-Translational, Ubiquitination, General Chemistry, Plant, chemistry, Gene Expression Regulation, Microscopy, Fluorescence, Mutation, Proteolysis, Vacuoles, biology.protein, High-harmonic generation, Protein Kinases, Protein Processing, Post-Translational, 010606 plant biology & botany
Abstract

Brassinosteroids (BRs) are plant steroid hormones that control many aspects of plant growth and development. BRs are perceived at the cell-surface by the plasma membrane-localized receptor complex composed of the receptor kinase BRI1 and its co-receptor BAK1. Here we show that BRI1 is post-translationally modified by K63 polyubiquitin chains in vivo. Artificially ubiquitinated BRI1 is recognized at the trans-Golgi Network/Early Endosomes (TGN/EE) and rapidly routed for vacuolar degradation. Mass spectrometry analyses identified residue K866 as an in vivo ubiquitination target in BRI1 involved in the negative regulation of BRI1. Model prediction revealed several redundant ubiquitination sites required for the endosomal sorting and vacuolar targeting of BRI1. Using total internal reflection fluorescence microscopy (TIRF), we also uncovered a role for BRI1 ubiquitination in promoting internalization from the cell-surface. Finally, we demonstrate that the control of BRI1 protein dynamics by ubiquitination is a fundamental control mechanism for BR responses in plants. Altogether, our results identify 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.

Published
2014
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