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160 results on '"Hem, Sonia"'

3. Convergent Evolution of Endosymbiont Differentiation in Dalbergioid and Inverted Repeat-Lacking Clade Legumes Mediated by Nodule-Specific Cysteine-Rich Peptides

Author

Czernic, Pierre, Gully, Djamel, Cartieaux, Fabienne, Moulin, Lionel, Guefrachi, Ibtissem, Patrel, Delphine, Pierre, Olivier, Fardoux, Joël, Chaintreuil, Clémence, Nguyen, Phuong, Gressent, Frédéric, Da Silva, Corinne, Poulain, Julie, Wincker, Patrick, Rofidal, Valérie, Hem, Sonia, Barrière, Quentin, Arrighi, Jean-François, Mergaert, Peter, and Giraud, Eric

Published
2015

8. Root Membrane Ubiquitinome under Short-Term Osmotic Stress

Author

Berger, Nathalie, primary, Demolombe, Vincent, additional, Hem, Sonia, additional, Rofidal, Valérie, additional, Steinmann, Laura, additional, Krouk, Gabriel, additional, Crabos, Amandine, additional, Nacry, Philippe, additional, Verdoucq, Lionel, additional, and Santoni, Véronique, additional

Published
2022
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10. Root membrane ubiquitinome under short-term osmotic stress

Author

Berger, Nathalie, primary, Demolombe, Vincent, additional, Hem, Sonia, additional, Rofidal, Valérie, additional, Steinmann, Laura, additional, Krouk, Gabriel, additional, Crabos, Amandine, additional, Nacry, Philippe, additional, Verdoucq, Lionel, additional, and Santoni, Véronique, additional

Published
2021
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15. Differential contribution of two organelles of endosymbiotic origin to iron-sulfur cluster synthesis in Toxoplasma

Author

Pamukcu, Sarah, Cerutti, Aude, Hem, Sonia, Rofidal, Valerie, Besteiro, Sébastien, LPHI - Laboratory of Pathogen Host Interactions (LPHI), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)

Subjects
bradyzoite, apicoplast, [SDV]Life Sciences [q-bio], mitochondrion, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, differentiation, iron sulfur cluster, Toxoplasma
Abstract

Iron-sulfur (Fe-S) clusters are one of the most ancient and ubiquitous prosthetic groups, and they are required by a variety of proteins involved in important metabolic processes. Apicomplexan parasites have inherited different plastidic and mitochondrial Fe-S clusters biosynthesis pathways through endosymbiosis. We have investigated the relative contributions of these pathways to the fitness of Toxoplasma gondii, an apicomplexan parasite causing disease in humans, by generating specific mutants. Phenotypic analysis and quantitative proteomics allowed us to highlight striking differences in these mutants. Both Fe-S cluster synthesis pathways are necessary for optimal parasite growth in vitro, but their disruption leads to markedly different fates: impairment of the plastidic pathway leads to a loss of the organelle and to parasite death, while disruption of the mitochondrial pathway trigger differentiation into a stress resistance stage. This highlights that otherwise similar biochemical pathways hosted by different sub-cellular compartments can have very different contributions to the biology of the parasites, which is something to consider when exploring novel strategies for therapeutic intervention.

Published
2021

17. Proteomic analysis of bystander effects in chondrosarcoma cells

Author

Gilbert, Antoine, Tudor, Mihaela, Lepleux, Charlotte, Rofidal, V., Hem, Sonia, Almunia, Christine, Armengaud, J., Brotin, Emilie, Haghdoost, Siamak, Savu, Diana, Chevalier, François, Accueil et Recherche en Radiobiologie des Ions Accélérés (ARIA), Centre de recherche sur les Ions, les MAtériaux et la Photonique (CIMAP - UMR 6252), Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU), Unité de Recherche Protéomique (PROTEOMIQUE), Institut National de la Recherche Agronomique (INRA), Plateforme de Spectrométrie de Masse Protéomique - Mass Spectrometry Proteomics Platform (MSPP), Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Innovations technologiques pour la Détection et le Diagnostic (LI2D), Service de Pharmacologie et Immunoanalyse (SPI), Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Médicaments et Technologies pour la Santé (MTS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Service de Pharmacologie et d'Immunoanalyse (SPI), Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Centre Régional de Lutte contre le Cancer François Baclesse [Caen] (UNICANCER/CRLC), UNICANCER-Tumorothèque de Caen Basse-Normandie (TCBN)-Normandie Université (NU), Department of Life and Environmental Physics [Magurele, Roumanie], Horia Hulubei National Institute of Physics and Nuclear Engineering [Magurele, Roumanie], Lund University, Swedish Radiobiological Society, Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche sur les Matériaux Avancés (IRMA), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-UNICANCER-Tumorothèque de Caen Basse-Normandie (TCBN), and Chevalier, Francois

Subjects
[SDV.CAN] Life Sciences [q-bio]/Cancer, [PHYS.PHYS.PHYS-BIO-PH] Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph], [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph], [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.CAN]Life Sciences [q-bio]/Cancer, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, ComputingMilieux_MISCELLANEOUS
Abstract

Numéro de Poster : P25; International audience

Published
2020

18. Technique ciblée Parallel Reaction Monitoring pour l’identification de protéines mineures

Author

Hem, Sonia, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Plateforme de Spectrométrie de Masse Protéomique - Mass Spectrometry Proteomics Platform (MSPP), and Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)

Subjects
[SDV]Life Sciences [q-bio], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2019

19. Coumarin accumulation and trafficking in Arabidopsis thaliana: a complex and dynamic process

Author

Robe, Kevin, primary, Conejero, Geneviève, additional, Gao, Fei, additional, Lefebvre‐Legendre, Linnka, additional, Sylvestre‐Gonon, Elodie, additional, Rofidal, Valérie, additional, Hem, Sonia, additional, Rouhier, Nicolas, additional, Barberon, Marie, additional, Hecker, Arnaud, additional, Gaymard, Frédéric, additional, Izquierdo, Esther, additional, and Dubos, Christian, additional

Published
2020
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21. P47. Proteomic analysis of the Radiation-Induced Bystander Effects between low-dose irradiated Chondrosarcoma cells and Bystander Chondrocytes

Author

Lepleux, Charlotte, Rofidal, Valerie, Hem, Sonia, Almunia, Christine, Armengaud, J., Chevalier, François, Accueil et Recherche en Radiobiologie des Ions Accélérés (ARIA), Centre de recherche sur les Ions, les MAtériaux et la Photonique (CIMAP - UMR 6252), Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU), Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Laboratoire Innovations technologiques pour la Détection et le Diagnostic (LI2D), Service de Pharmacologie et Immunoanalyse (SPI), Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Médicaments et Technologies pour la Santé (MTS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Service de Pharmacologie et d'Immunoanalyse (SPI), Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche sur les Matériaux Avancés (IRMA), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Chevalier, Francois

Subjects
[SDV.CAN] Life Sciences [q-bio]/Cancer, [PHYS.PHYS.PHYS-BIO-PH] Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph], [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph], [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BV] Life Sciences [q-bio]/Vegetal Biology, [SDV.CAN]Life Sciences [q-bio]/Cancer, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2019

22. Seed comparative genomics in three coffee species identify desiccation tolerance mechanisms in intermediate seeds

Author

Stavrinides, Anna K., Dussert, Stéphane, Combes, Marie-Christine, Fock-Bastide, Isabelle, Severac, Dany, Minier, Jérôme, Bastos-Siqueira, Aldecinei, Demolombe, Vincent, Hem, Sonia, Lashermes, Philippe, Joët, Thierry, Stavrinides, Anna K., Dussert, Stéphane, Combes, Marie-Christine, Fock-Bastide, Isabelle, Severac, Dany, Minier, Jérôme, Bastos-Siqueira, Aldecinei, Demolombe, Vincent, Hem, Sonia, Lashermes, Philippe, and Joët, Thierry

Abstract

In contrast to desiccation-tolerant 'orthodox' seeds, so-called 'intermediate' seeds cannot survive complete drying and are short-lived. All species of the genus Coffea produce intermediate seeds, but they show a considerable variability in seed desiccation tolerance (DT), which may help to decipher the molecular basis of seed DT in plants. We performed a comparative transcriptome analysis of developing seeds in three coffee species with contrasting desiccation tolerance. Seeds of all species shared a major transcriptional switch during late maturation that governs a general slow-down of metabolism. However, numerous key stress-related genes, including those coding for the late embryogenesis abundant protein EM6 and the osmosensitive calcium channel ERD4, were up-regulated during DT acquisition in the two species with high seed DT, C. arabica and C. eugenioides. By contrast, we detected up-regulation of numerous genes involved in the metabolism, transport, and perception of auxin in C. canephora seeds with low DT. Moreover, species with high DT showed a stronger down-regulation of the mitochondrial machinery dedicated to the tricarboxylic acid cycle and oxidative phosphorylation. Accordingly, respiration measurements during seed dehydration demonstrated that intermediate seeds with the highest DT are better prepared to cease respiration and avoid oxidative stresses.

Published
2019

23. Phosphoproteomic analysis reveals major default phosphorylation sites outside long intrinsically disordered regions of Arabidopsis plasma membrane proteins

Author

Nespoulous Claude, Rofidal Valérie, Sommerer Nicolas, Hem Sonia, and Rossignol Michel

Subjects
Arabidopsis, Plasma membrane, Phosphoproteome, Intrinsically disordered regions, Cytology, QH573-671
Abstract

Abstract Background Genome-wide statistics established that long intrinsically disordered regions (over 30 residues) are predicted in a large part of proteins in all eukaryotes, with a higher ratio in trans-membrane proteins. At functional level, such unstructured and flexible regions were suggested for years to favour phosphorylation events. In plants, despite increasing evidence of the regulation of transport and signalling processes by phosphorylation events, only few data are available without specific information regarding plasma membrane proteins, especially at proteome scale. Results Using a dedicated phosphoproteomic workflow, 75 novel and unambiguous phosphorylation sites were identified in Arabidopsis plasma membrane. Bioinformatics analysis showed that this new dataset concerned mostly integral proteins involved in key functions of the plasma membrane (such as transport and signal transduction, including protein phosphorylation). It thus expanded by 15% the directory of phosphosites previously characterized in signalling and transport proteins. Unexpectedly, 66% of phosphorylation sites were predicted to be located outside long intrinsically disordered regions. This result was further corroborated by analysis of publicly available data for the plasma membrane. Conclusions The new phosphoproteomics data presented here, with published datasets and functional annotation, suggest a previously unexpected topology of phosphorylation in the plant plasma membrane proteins. The significance of these new insights into the so far overlooked properties of the plant plasma membrane phosphoproteome and the long disordered regions is discussed.

Published
2012
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24. Decrypting the chloroplastic [fe-s] cluster assembly machinery

Author

Berger, Nathalie, Touraine, Brigitte, Magno, Cyril, Hem, Sonia, Rofidal, Valerie, Demolombe - Liozu, Vincent, Vignols, Florence, Rouhier, Nicolas, Feussner, Kristin, Ischebeck, Till, Zienkiewicz, Krzysztof, Feussner, Ivo, Santoni, Veronique, Gaymard, Frederic, Dubos, Christian, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Interactions Arbres-Microorganismes (IAM), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Department of Plant Biochemistry, Lund University [Lund], University of Goettingen, Goettingen Metabolomics and Lipidomics Laboratory, Goettingen Center for Molecular Biosciences (GZMB ), University Medicine Goettingen, GGoettingen Center for Molecular Biosciences, Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), University of Göttingen - Georg-August-Universität Göttingen, and University Medical Center Göttingen (UMG)

Subjects
arabidopsis, chlorophylle, sulphur protein, protéine, activité mitochondriale, protéine soufrée, homéostasie du fer, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, chlorophyll, sulphur s (symbol), approche protéomique, protein, soufre
Abstract

Iron-Sulfur ([Fe-S]) clusters are metal cofactors of proteins involved in many fundamental metabolic pathways and cellular processes occurring in both prokaryotes and eukaryotes ( e.g. respiration, photosynthesis). [Fe-S] clusters participate in electrontransfer, substrate binding/activation, iron and sulfur storage, regulation of gene expression, and enzyme activity. The [Fe-S] cluster biogenesis machinery is composed of scaffold proteins that build the cluster de novo and of carrier proteins that transfer the [Fe-S] prosthetic groups to their target proteins (also called apoproteins). In plants three different machineries lead to [Fe-S] cluster assembly, namely the mitochondrial ISC (Iron Sulfer Cluster) system, the chloroplastic SUF (SUlFur mobilization) system and the cytosolic CIA (Cytosolic Iron-sulfur cluster Assembly) system. Our team focuses mainly on the chloroplastic SUF system and specifically on the characterization of a [Fe-S] carrier proteins named NFU2 ( NiFU-LIKE PROTEIN 2) and its potential role on the maturation of the 45 putative chloroplastic [Fe-S] cluster proteins. The [Fe-S] cluster acquisition of only 5 targets among the 45 putative chloroplastic [Fe-S] cluster proteins has already been explored. Thus, the identification of the carriers that act on the other 40 targets is still a big challenge. In order to shed new light on this process, we have initiated the global characterisation of the nfu2 mutant using proteomic (quantitative label free mass-spectrometry strategy) and metabolomic approaches. Results obtained within the frame of this work will be discussed.

Published
2018

25. Targeted Proteomics Allows Quantification of Ethylene Receptors and Reveals SlETR3 Accumulation in Never-Ripe Tomatoes

Author

Chen, Yi, primary, Rofidal, Valérie, additional, Hem, Sonia, additional, Gil, Julie, additional, Nosarzewska, Joanna, additional, Berger, Nathalie, additional, Demolombe, Vincent, additional, Bouzayen, Mondher, additional, Azhar, Beenish J., additional, Shakeel, Samina N., additional, Schaller, G. Eric, additional, Binder, Brad M., additional, Santoni, Véronique, additional, and Chervin, Christian, additional

Published
2019
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26. NRT2.1 phosphorylation prevents root high affinity nitrate uptake activity inArabidopsis thaliana

Author

Jacquot, Aurore, primary, Chaput, Valentin, additional, Mauries, Adeline, additional, Li, Zhi, additional, Tillard, Pascal, additional, Fizames, Cécile, additional, Bonillo, Pauline, additional, Bellegarde, Fanny, additional, Laugier, Edith, additional, Santoni, Véronique, additional, Hem, Sonia, additional, Martin, Antoine, additional, Gojon, Alain, additional, Schulze, Waltraud, additional, and Lejay, Laurence, additional

Published
2019
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27. Coumarin accumulation and trafficking in Arabidopsis thaliana: a complex and dynamic process.

Author

Robe, Kevin, Conejero, Geneviève, Gao, Fei, Lefebvre‐Legendre, Linnka, Sylvestre‐Gonon, Elodie, Rofidal, Valérie, Hem, Sonia, Rouhier, Nicolas, Barberon, Marie, Hecker, Arnaud, Gaymard, Frédéric, Izquierdo, Esther, and Dubos, Christian

Subjects
PLANT roots, COUMARINS, PLANT species, SCOPOLETIN, PLANT growth
Abstract

Summary: Iron (Fe) is a major micronutrient and is required for plant growth and development. Nongrass species have evolved a reduction‐based strategy to solubilize and take up Fe. The secretion of Fe‐mobilizing coumarins (e.g. fraxetin, esculetin and sideretin) by plant roots plays an important role in this process. Although the biochemical mechanisms leading to their biosynthesis have been well described, very little is known about their cellular and subcellular localization or their mobility within plant tissues.Spectral imaging was used to monitor, in Arabidopsis thaliana, the in planta localization of Fe‐mobilizing coumarins and scopolin. Molecular, genetic and biochemical approaches were also used to investigate the dynamics of coumarin accumulation in roots.These approaches showed that root hairs play a major role in scopoletin secretion, whereas fraxetin and esculetin secretion occurs through all epidermis cells. The findings of this study also showed that the transport of coumarins from the cortex to the rhizosphere relies on the PDR9 transporter under Fe‐deficient conditions. Additional experiments support the idea that coumarins move throughout the plant body via the xylem sap and that several plant species can take up coumarins present in the surrounding media.Altogether, the data presented here demonstrate that coumarin storage and accumulation in roots is a highly complex and dynamic process. [ABSTRACT FROM AUTHOR]

Published
2021
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28. Interactomics reveals novel regulatory mechanisms of plant aquaporins

Author

BELLATI, Jorge, Champeyroux, Chloé, Hem, Sonia, Rofidal, Valerie, Krouk, Gabriel, Maurel, Christophe, Santoni, Veronique, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

Subjects
aquaporin, water stress, arabidopsis, protéine racinaire de stress hydrique, aquaporine, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, stress hydrique
Abstract

Interactomics reveals novel regulatory mechanisms of plant aquaporins. Congrès Spectrométrie de Masse, Métabolomique et Analyse Protéomique (SMMAP)

Published
2017

29. Seed comparative genomics in three coffee species identify desiccation tolerance mechanisms in intermediate seeds.

Author

Stavrinides, Anna K, Dussert, Stéphane, Combes, Marie-Christine, Fock-Bastide, Isabelle, Severac, Dany, Minier, Jérôme, Bastos-Siqueira, Aldecinei, Demolombe, Vincent, Hem, Sonia, Lashermes, Philippe, and Joët, Thierry

Subjects
COMPARATIVE genomics, AUXIN, KREBS cycle, SEEDS, RESPIRATORY measurements, CALCIUM channels, OXIDATIVE phosphorylation
Abstract

In contrast to desiccation-tolerant 'orthodox' seeds, so-called 'intermediate' seeds cannot survive complete drying and are short-lived. All species of the genus Coffea produce intermediate seeds, but they show a considerable variability in seed desiccation tolerance (DT), which may help to decipher the molecular basis of seed DT in plants. We performed a comparative transcriptome analysis of developing seeds in three coffee species with contrasting desiccation tolerance. Seeds of all species shared a major transcriptional switch during late maturation that governs a general slow-down of metabolism. However, numerous key stress-related genes, including those coding for the late embryogenesis abundant protein EM6 and the osmosensitive calcium channel ERD4, were up-regulated during DT acquisition in the two species with high seed DT, C. arabica and C. eugenioides. By contrast, we detected up-regulation of numerous genes involved in the metabolism, transport, and perception of auxin in C. canephora seeds with low DT. Moreover, species with high DT showed a stronger down-regulation of the mitochondrial machinery dedicated to the tricarboxylic acid cycle and oxidative phosphorylation. Accordingly, respiration measurements during seed dehydration demonstrated that intermediate seeds with the highest DT are better prepared to cease respiration and avoid oxidative stresses. [ABSTRACT FROM AUTHOR]

Published
2020
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30. Phosphoproteomics and interactomics reveal novel regulatory mechanisms of plant aquaporins

Author

BELLATI, Jorge, Di Pietro, Magali, Prado, Karine, Champeyroux, Chloé, Rofidal, Valerie, Hem, Sonia, Maurel, Christophe, Santoni, Veronique, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

Subjects
aquaporin, arabidopsis, aquaporine, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, interactome, mécanisme de régulation, protéomique quantitative
Abstract

Phosphoproteomics and interactomics reveal novel regulatory mechanisms of plant aquaporins. Congrès de la Société Française d'Electrophorèse et d'Analyse Protéomique (SFEAP)

Published
2016

31. Regulation in primary metabolism of transgenic maize endosperm after metabolic engineering of astaxanthin biosynthesis highlighted by a label-free quantitative proteomics strategy

Author

DECOURCELLE, Mathilde, Rofidal, Valerie, Santoni, Veronique, Hem, Sonia, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Plateforme de Spectrométrie de Masse Protéomique - Mass Spectrometry Proteomics Platform (MSPP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

Subjects
ingénierie métabolique, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, astaxanthine, metabolic engineering, maïs transgénique, protéomique quantitative
Abstract

Regulation in primary metabolism of transgenic maize endosperm after metabolic engineering of astaxanthin biosynthesis highlighted by a label-free quantitative proteomics strategy. 33. Congrès de la Société Française d'Electrophorèse et d'Analyse Protéomique (SFEAP)

Published
2016

32. Post-translational regulation of the root nitrate uptake transporter NRT2.1 in A rabidopsis thaliana

Author

Jacquot, Aurore, Mauries, Adeline, LAUGIER, Edith, Hem, Sonia, Rofidal, Valerie, Tillard, Pascal, Santoni, Veronique, Schulze, Waltraud, Gojon, Alain, Lejay-Lefebvre, Laurence, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Plateforme de Spectrométrie de Masse Protéomique - Mass Spectrometry Proteomics Platform (MSPP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

Subjects
[SDV]Life Sciences [q-bio], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2016

34. The cell proliferation antigen Ki-67 organises heterochromatin

Author

Sobecki, Michal, David, Alexandre, Eguren, Manuel, Birling, Marie Christine, Urbach, Serge, Hem, Sonia, Déjardin, Jérôme, Malumbres, Marcos, Jay, Philippe, Dulic, Vjekoslav, Lafontaine, Denis, Mrouj, Karim, Feil, Robert, Fisher, Daniel, Camasses, Alain, Parisis, Nikolaos, Nicolas, Emilien, Llères, David, Gerbe, François, Prieto, Susana, Krasinska, Liliana, Sobecki, Michal, David, Alexandre, Eguren, Manuel, Birling, Marie Christine, Urbach, Serge, Hem, Sonia, Déjardin, Jérôme, Malumbres, Marcos, Jay, Philippe, Dulic, Vjekoslav, Lafontaine, Denis, Mrouj, Karim, Feil, Robert, Fisher, Daniel, Camasses, Alain, Parisis, Nikolaos, Nicolas, Emilien, Llères, David, Gerbe, François, Prieto, Susana, and Krasinska, Liliana

Abstract

Antigen Ki-67 is a nuclear protein expressed in proliferating mammalian cells. It is widely used in cancer histopathology but its functions remain unclear. Here, we show that Ki-67 controls heterochromatin organisation. Altering Ki-67 expression levels did not significantly affect cell proliferation in vivo. Ki-67 mutant mice developed normally and cells lacking Ki-67 proliferated efficiently. Conversely, upregulation of Ki-67 expression in differentiated tissues did not prevent cell cycle arrest. Ki-67 interactors included proteins involved in nucleolar processes and chromatin regulators. Ki-67 depletion disrupted nucleologenesis but did not inhibit pre-rRNA processing. In contrast, it altered gene expression. Ki-67 silencing also had wide-ranging effects on chromatin organisation, disrupting heterochromatin compaction and long-range genomic interactions. Trimethylation of histone H3K9 and H4K20 was relocalised within the nucleus. Finally, overexpression of human or Xenopus Ki-67 induced ectopic heterochromatin formation. Altogether, our results suggest that Ki-67 expression in proliferating cells spatially organises heterochromatin, thereby controlling gene expression., SCOPUS: ar.j, info:eu-repo/semantics/published

Published
2016

35. Quantitative proteomics unravels novel post-translational regulatory mechanisms of plant aquaporins

Author

Di Pietro, Magali, Vialaret, Jérôme, Li, Guowei, Hem, Sonia, Prado, Karine, Maurel, Christophe, Santoni, Veronique, Biochimie et Physiologie Moléculaire des Plantes (BPMP), and Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology
Abstract

absent

Published
2014

36. Variations of carotenoid pathways in transgenic maize endosperms highlighted by a Label-Free quantitative proteomics approach

Author

DECOURCELLE, Mathilde, Duval, Jérémy, Chouiki Alilou, Hajar, Rofidal, Valerie, Santoni, Veronique, Hem, Sonia, ProdInra, Archive Ouverte, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Amélioration génétique et adaptation des plantes méditerranéennes et tropicales (UMR AGAP), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), and Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)

Subjects
[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT], [SDV.OT] Life Sciences [q-bio]/Other [q-bio.OT], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, food and beverages, [SDV.BV] Life Sciences [q-bio]/Vegetal Biology
Abstract

b-carotene and astaxanthin that are mainly produced by chemical synthesis constitute typical supplement feed for poultries and fishes. The project CaroMaize (ANR program Plant-KBBE) proposes to use transgenic maize seeds expressing high level of carotenoids, obtained by metabolic engineering of biosynthesis pathway (Zhu et al.) as a raw source for industry and animal feeding. In addition to metabolomics analyses including the characterization of carotenoids profiles, transgenic maize lines are subjected to integrated transcriptomics and proteomics approach. As such, the proteomic profile of endosperm from transgenic plants enriched in b-carotene and astaxanthin was compared to that of a control genotype. A quantitative label-free proteomics analysis of total protein extracts allowed us to establish a first endosperm protein directory, to describe its functional characteristics and to characterize proteins with significant variations between genotypes highlighting putative variations of the carotenoids pathway.

Published
2014

38. The cell proliferation antigen Ki-67 organises heterochromatin

Author

Sobecki, Michal, primary, Mrouj, Karim, additional, Camasses, Alain, additional, Parisis, Nikolaos, additional, Nicolas, Emilien, additional, Llères, David, additional, Gerbe, François, additional, Prieto, Susana, additional, Krasinska, Liliana, additional, David, Alexandre, additional, Eguren, Manuel, additional, Birling, Marie-Christine, additional, Urbach, Serge, additional, Hem, Sonia, additional, Déjardin, Jérôme, additional, Malumbres, Marcos, additional, Jay, Philippe, additional, Dulic, Vjekoslav, additional, Lafontaine, Denis LJ, additional, Feil, Robert, additional, and Fisher, Daniel, additional

Published
2016
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39. Author response: The cell proliferation antigen Ki-67 organises heterochromatin

Author

Sobecki, Michal, primary, Mrouj, Karim, additional, Camasses, Alain, additional, Parisis, Nikolaos, additional, Nicolas, Emilien, additional, Llères, David, additional, Gerbe, François, additional, Prieto, Susana, additional, Krasinska, Liliana, additional, David, Alexandre, additional, Eguren, Manuel, additional, Birling, Marie-Christine, additional, Urbach, Serge, additional, Hem, Sonia, additional, Déjardin, Jérôme, additional, Malumbres, Marcos, additional, Jay, Philippe, additional, Dulic, Vjekoslav, additional, Lafontaine, Denis LJ, additional, Feil, Robert, additional, and Fisher, Daniel, additional

Published
2016
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40. Differential expression of midgut proteins in Trypanosomae brucei gambiense-stimulated vs. non-stimulated Glossina palpalis gambiensis flies

Author

Geiger, Anne, Soumana, Illiassou Hamidou, Tchicaya, Bernadette, Rofidal, Valérie, Decourcelles, Mathilde, Santoni, Sylvain, Hem, Sonia, Geiger, Anne, Soumana, Illiassou Hamidou, Tchicaya, Bernadette, Rofidal, Valérie, Decourcelles, Mathilde, Santoni, Sylvain, and Hem, Sonia

Abstract

The unicellular pathogenic protozoan Trypanosoma brucei gambiense is responsible for the chronic form of sleeping sickness. This vector-borne disease is transmitted to humans by the tsetse fly of the group Glossina palpalis, including the subspecies G. p. gambiensis, in which the parasite completes its developmental cycle. Sleeping sickness control strategies can therefore target either the human host or the fly vector. Indeed, suppression of one step in the parasite developmental cycle could abolish parasite transmission to humans, with consequences on the spreading of the disease. In order to develop this type of approach, we have identified, at the proteome level, events resulting from the tripartite interaction between the tsetse fly G. p. gambiensis, its microbiome, and the trypanosome. Proteomes were analyzed from four biological replicates of midguts from flies sampled 3 days post-feeding on either a trypanosome-infected (stimulated flies) or a non-infected (non-stimulated flies) bloodmeal. Over 500 proteins were identified in the midguts of flies from both feeding groups, 13 of which were shown to be differentially expressed in trypanosome-stimulated vs. non-stimulated flies. Functional annotation revealed that several of these proteins have important functions that could be involved in modulating the fly infection process by trypanosomes (and thus fly vector competence), including anti-oxidant and anti-apoptotic, cellular detoxifying, trypanosome agglutination, and immune stimulating or depressive effects. The results show a strong potential for diminishing or even disrupting fly vector competence, and their application holds great promise for improving the control of sleeping sickness.

Published
2015

41. Efficient and unbiased extraction and quantification of soil proteins - the first step to characterization

Author

Staunton, Siobhan, Jorge Araujo, Priscila, Amenc, Laurie, Hem, Sonia, Santoni, Veronique, Quiquampoix, Herve, Ecologie fonctionnelle et biogéochimie des sols et des agro-écosystèmes (UMR Eco&Sols), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Institut National de la Recherche Agronomique (INRA), Science Without Borders, Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Institut National de la Recherche Agronomique (INRA)-Institut de Recherche pour le Développement (IRD)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV]Life Sciences [q-bio]
Abstract

Given the adsorption capacity of soils and the strong tendency of proteins to adsorb to surfaces, it is thus not surprising that the extraction yield of soil proteins is often poor. Given the heterogeneity of soils and the proteins they contain, it is likely that no simple recipe can ever be found to extract all proteins from all soils so that they can be quantified and characterized. We will describe some of the approaches we have used to extract soil proteins, to quantify the protein in extracts, to assess various purification steps. In general protein desorption is favored by alkaline pH, the presence of surfactants and the addition of other proteins to compete for soil surfaces. Alkaline pH leads to the co-extraction of polyphenols that may complex with proteins and interfere with quantification and separation by SDS-PAGE. It proves difficult to separate proteins and polyphenols by the standard technique of acid precipitation and some extraction conditions appear to lead to the formation of stable complexes. Surfactants are incompatible with the commonly used Bradford assay and have to be removed prior to analysis, with the risk of loss of protein. The addition of a known protein increases soil protein extraction yield by surface exchange. Although large protein addition is not suited to a subsequent proteomic analysis of samples, this approach can be used to extract targeted proteins, for which specific assays of concentration (e.g. immune-assays) or function (e.g. catalytic activity) exist.

Published
2013

42. Coordinated post-translational responses of aquaporins to abiotic and nutritional stimuli in Arabidopsis roots

Author

Santoni, Veronique, Di Pietro, Magali, Vialaret, Jérôme, Li, Guowei, Hem, Sonia, Rossignol, Michel, Maurel, Christophe, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Unité de Recherche Protéomique (PROTEOMIQUE), Institut National de la Recherche Agronomique (INRA), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), and ProdInra, Archive Ouverte

Subjects
[SDV] Life Sciences [q-bio], aquaporin, physiologie végétale, arabidopsis, absorption racinaire, résistance à l'inondation, [SDV]Life Sciences [q-bio], aquaporine, root absorption
Abstract

Coordinated post-translational responses of aquaporins to abiotic and nutritional stimuli in Arabidopsis roots . 7th European Plant Science Organisation (EPSO) Conference

Published
2013

43. Control of Arabidopsis leaf hydraulics involves light-dependent phosphorylation of aquaporins in veins

Author

Prado, Karine, Boursiac, Yann, Tournaire-Roux, Colette, Monneuse, Jean-Marc, Postaire, Olivier, Da Ines, Olivier, Schaffner, Anton R., Hem, Sonia, Santoni, Veronique, Maurel, Christophe, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Unité de Recherche Protéomique (PROTEOMIQUE), Institut National de la Recherche Agronomique (INRA), Institute of Biochemical Plant Pathology, German Research Center for Environmental Health - Helmholtz Center München (GmbH), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)

Subjects
aquaporin, arabidopsis, résistance à l'inondation, fungi, education, food and beverages, aquaporine, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, photobiology, photobiologie, humanities, health care economics and organizations, distribution de l'eau
Abstract

Control of Arabidopsis leaf hydraulics involves light-dependent phosphorylation of aquaporins in veins. International Symposium on Plant Photobiology

Published
2013

47. Multiple phosphorylations in the C-terminal tail of plant plasma membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in response to salt stress

Author

Prak, Sodana, Hem, Sonia, Boudet, Julie, Viennois, Gaëlle, Sommerer, Nicolas, Rossignol, Michel, Maurel, Christophe, Santoni, Véronique, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Protéomique Fonctionnelle (LPF), Institut National de la Recherche Agronomique (INRA), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), and Unité de Recherche Protéomique (PROTEOMIQUE)

Subjects
channel proteins, expression génique, water, Aquaporins, plasma membrane, Plant Roots, Mass Spectrometry, Serine, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, transport membranaire, Phosphorylation, Plant Physiological Phenomena, salinité, Plant Proteins, stress abiotique, Binding Sites, AQUAPORIN, CHANNEL PROTEINS, WATER TRANSPORT, PLASMA MEMBRANE, SALT STRESS, Arabidopsis Proteins, Aquaporin, ACL, Cell Membrane, aquaporine, Plants, Genetically Modified, root, Protein Structure, Tertiary, arabidopsis, AtPIPs, transport, Salts, Peptides
Abstract

Article recommandé par Faculty of 1000 Biology; Aquaporins form a family of water and solute channel proteins and are present in most living organisms. In plants, aquaporins play an important role in the regulation of root water transport in response to abiotic stresses. In this work, we investigated the role of phosphorylation of plasma membrane intrinsic protein (PIP) aquaporins in the Arabidopsis thaliana root by a combination of quantitative mass spectrometry and cellular biology approaches. A novel phosphoproteomics procedure that involves plasma membrane purification, phosphopeptide enrichment with TiO(2) columns, and systematic mass spectrometry sequencing revealed multiple and adjacent phosphorylation sites in the C-terminal tail of several AtPIPs. Six of these sites had not been described previously. The phosphorylation of AtPIP2;1 at two C-terminal sites (Ser(280) and Ser(283)) was monitored by an absolute quantification method and shown to be altered in response to treatments of plants by salt (NaCl) and hydrogen peroxide. The two treatments are known to strongly decrease the water permeability of Arabidopsis roots. To investigate a putative role of Ser(280) and Ser(283) phosphorylation in aquaporin subcellular trafficking, AtPIP2;1 forms mutated at either one of the two sites were fused to the green fluorescent protein and expressed in transgenic plants. Confocal microscopy analysis of these plants revealed that, in resting conditions, phosphorylation of Ser(283) is necessary to target AtPIP2;1 to the plasma membrane. In addition, an NaCl treatment induced an intracellular accumulation of AtPIP2;1 by exerting specific actions onto AtPIP2;1 forms differing in their phosphorylation at Ser(283) to induce their accumulation in distinct intracellular structures. Thus, the present study documents stress-induced quantitative changes in aquaporin phosphorylation and establishes for the first time a link with plant aquaporin subcellular localization.

Published
2008

48. Caractérisation par spectrométrie de masse de réponses précoces du phosphoprotéome d'Arabidopsis thaliana au stress en fer

Author

Hem, Sonia, Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Université Montpellier 2 (Sciences et Techniques), Jean-François BRIAT, and Michel ROSSIGNOL

Subjects
stress, phosphoprotéomique, MALDI-TOF/TOF MS/MS, Arabidopsis, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, membrane plasmique, protéomique, fer
Abstract

Chez les plantes soumises à un excès de fer, l'induction des ferritines constitue la réponse moléculaire la mieux caractérisée. Ce processus est contrôlé par des étapes de (dé)phosphorylation de protéines. L'objectif de ce travail était de caractériser les variations du phosphoprotéome de cellules d'Arabidopsis cultivées dans différentes conditions de nutrition en fer pour révéler les acteurs moléculaires impliqués dans ces évènements précoces. L'essentiel de l'approche a été réalisé directement à partir des peptides. La stratégie générale a consisté à d'abord optimiser, sur des mélanges de protéines modèles de complexité croissante, des procédures de purification et de tri des peptides phosphorylés, puis à appliquer ces démarches aux situations biologiques d'intérêt. Dans chaque cas, l'identification des sites de phosphorylation a été réalisée par MS/MS, de type MALDI-TOF/TOF ou nanoLC-ESI. Parmi les méthodes développées, la combinaison d'un enrichissement initial par interaction avec du TiO2, d'un fractionnement par échange d'anion et d'une purification finale sur dioxyde de titane, s'est avérée la plus performante pour les mélanges complexes de phosphopeptides. Cette méthode a ensuite été appliquée aux peptides excisés de la face cytoplasmique de la membrane plasmique. Elle a permis d'identifier des sites pS et pT sur des peptides mono- et multi-phosphorylés de diverses protéines membranaires d'Arabidopsis. Parmi les phosphoprotéines identifiées, une partie majeure correspond à des transporteurs ou à des kinases, et un tiers des sites de phosphorylation n'avaient jamais été décrits. Diverses approches de marquage (métabolique, chimique, protéolytique) ont ensuite été adaptées pour quantifier les variations cinétiques de ces sites au cours de la réponse au stress. L'estimation des changements de niveaux de phosphorylation a été réalisé en spectrométrie de masse après fractionnement et enrichissement des peptides comme décrit ci-dessus.

Published
2008

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