المؤلفون: Chen Liu, Andriani Mentzelopoulou, Fotini Papagavriil, Prashanth Ramachandran, Artemis Perraki, Lucas Claus, Sebastian Barg, Peter Dörmann, Yvon Jaillais, Philipp Johnen, Eugenia Russinova, Electra Gizeli, Gabriel Schaaf, Panagiotis Nikolaou Moschou

المصدر: PLoS Biology, Vol 21, Iss 9, p e3002305 (2023)

مصطلحات موضوعية: Biology (General), QH301-705.5

الوصف: Protein function can be modulated by phase transitions in their material properties, which can range from liquid- to solid-like; yet, the mechanisms that drive these transitions and whether they are important for physiology are still unknown. In the model plant Arabidopsis, we show that developmental robustness is reinforced by phase transitions of the plasma membrane-bound lipid-binding protein SEC14-like. Using imaging, genetics, and in vitro reconstitution experiments, we show that SEC14-like undergoes liquid-like phase separation in the root stem cells. Outside the stem cell niche, SEC14-like associates with the caspase-like protease separase and conserved microtubule motors at unique polar plasma membrane interfaces. In these interfaces, SEC14-like undergoes processing by separase, which promotes its liquid-to-solid transition. This transition is important for root development, as lines expressing an uncleavable SEC14-like variant or mutants of separase and associated microtubule motors show similar developmental phenotypes. Furthermore, the processed and solidified but not the liquid form of SEC14-like interacts with and regulates the polarity of the auxin efflux carrier PINFORMED2. This work demonstrates that robust development can involve liquid-to-solid transitions mediated by proteolysis at unique plasma membrane interfaces.

وصف الملف: electronic resource

العلاقة: https://journals.plos.org/plosbiology/article/file?id=10.1371/journal.pbio.3002305&type=printableTest; https://doaj.org/toc/1544-9173Test; https://doaj.org/toc/1545-7885Test

الوصول الحر: https://doaj.org/article/e2a44caa675b4120a3b674204b069a27Test

المؤلفون: Artemis Perraki, Julien Gronnier, Paul Gouguet, Marie Boudsocq, Anne-Flore Deroubaix, Vincent Simon, Sylvie German-Retana, Anthony Legrand, Birgit Habenstein, Cyril Zipfel, Emmanuelle Bayer, Sébastien Mongrand, Véronique Germain

المصدر: PLoS Pathogens, Vol 14, Iss 11, p e1007378 (2018)

مصطلحات موضوعية: Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5

الوصف: Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3's phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.

وصف الملف: electronic resource

العلاقة: http://europepmc.org/articles/PMC6258466?pdf=renderTest; https://doaj.org/toc/1553-7366Test; https://doaj.org/toc/1553-7374Test

الوصول الحر: https://doaj.org/article/941c02dd27dc4e40aedaf8c72766e69eTest

المؤلفون: Vijayata Singh, Artemis Perraki, Sang Y. Kim, Stuti Shrivastava, Jae H. Lee, Youfu Zhao, Benjamin Schwessinger, Man-Ho Oh, Amy Marshall-Colon, Cyril Zipfel, Steven C. Huber

المصدر: Frontiers in Plant Science, Vol 8 (2017)

مصطلحات موضوعية: receptor kinase, co-receptor, innate immunity, growth, brassinosteroid, pathogen-associated molecular pattern, Plant culture, SB1-1110

الوصف: The plasma membrane-localized BRI1-ASSOCIATED KINASE1 (BAK1) functions as a co-receptor with several receptor kinases including the brassinosteroid (BR) receptor BRASSINOSTEROID-INSENSITIVE 1 (BRI1), which is involved in growth, and the receptors for bacterial flagellin and EF-Tu, FLAGELLIN-SENSING 2 (FLS2) and EF-TU RECEPTOR (EFR), respectively, which are involved in immunity. BAK1 is a dual specificity protein kinase that can autophosphorylate on serine, threonine and tyrosine residues. It was previously reported that phosphorylation of Tyr-610 in the carboxy-terminal domain of BAK1 is required for its function in BR signaling and immunity. However, the functional role of Tyr-610 in vivo has recently come under scrutiny. Therefore, we have generated new BAK1 (Y610F) transgenic plants for functional studies. We first produced transgenic Arabidopsis lines expressing BAK1 (Y610F)-Flag in the homozygous bak1-4 bkk1-1 double null background. In a complementary approach, we expressed untagged BAK1 and BAK1 (Y610F) in the bak1-4 null mutant. Neither BAK1 (Y610F) transgenic line had any obvious growth phenotype when compared to wild-type BAK1 expressed in the same background. In addition, the BAK1 (Y610F)-Flag plants responded similarly to plants expressing BAK1-Flag in terms of brassinolide (BL) inhibition of root elongation, and there were only minor changes in gene expression between the two transgenic lines as monitored by microarray analysis and quantitative real-time PCR. In terms of plant immunity, there were no significant differences between plants expressing BAK1 (Y610F)-Flag and BAK1-Flag in the growth of the non-pathogenic hrpA- mutant of Pseudomonas syringae pv. tomato DC3000. Furthermore, untagged BAK1 (Y610F) transgenic plants were as responsive as plants expressing BAK1 (in the bak1-4 background) and wild-type Col-0 plants toward treatment with the EF-Tu- and flagellin-derived peptide epitopes elf18- and flg22, respectively, as measured by reactive oxygen species production, mitogen-activated protein kinase activation, and seedling growth inhibition. These new results do not support any involvement of Tyr-610 phosphorylation in either BR or immune signaling.

وصف الملف: electronic resource

العلاقة: http://journal.frontiersin.org/article/10.3389/fpls.2017.01273/fullTest; https://doaj.org/toc/1664-462XTest

الوصول الحر: https://doaj.org/article/15e71d0fdbab4d24a4f4855eb3062f20Test

المؤلفون: Eftychios Frangedakis (8662560), Fernando Guzman-Chavez (10933751), Marius Rebmann (8662563), Kasey Markel (8662569), Ying Yu (7066), Artemis Perraki (5954828), Sze Wai Tse (10933754), Yang Liu (4829), Jenna Rever (10933757), Susanna Sauret-Gueto (10933760), Bernard Goffinet (542070), Harald Schneider (9541), Jim Haseloff (91083)

مصطلحات موضوعية: Biochemistry, Genetics, Molecular Biology, Ecology, Developmental Biology, Plant Biology, Biological Sciences not elsewhere classified, Candidate binding sites, 51 bryophyte species, transformation, Marchantia chloroplasts, liverwort Marchantia polymorpha, reporter gene expression, protein hyperexpression, chloroplast post-transcriptional re., mRNA, Marchantia Chloroplasts Chloroplasts, novel DNA tools

الوصف: Chloroplasts are attractive platforms for synthetic biology applications since they are capable of driving very high levels of transgene expression, if mRNA production and stability are properly regulated. However, plastid transformation is a slow process and currently limited to a few plant species. The liverwort Marchantia polymorpha is a simple model plant that allows rapid transformation studies; however, its potential for protein hyperexpression has not been fully exploited. This is partially due to the fact that chloroplast post-transcriptional regulation is poorly characterized in this plant. We have mapped patterns of transcription in Marchantia chloroplasts. Furthermore, we have obtained and compared sequences from 51 bryophyte species and identified putative sites for pentatricopeptide repeat protein binding that are thought to play important roles in mRNA stabilization. Candidate binding sites were tested for their ability to confer high levels of reporter gene expression in Marchantia chloroplasts, and levels of protein production and effects on growth were measured in homoplastic transformed plants. We have produced novel DNA tools for protein hyperexpression in this facile plant system that is a test-bed for chloroplast engineering.

العلاقة: https://figshare.com/articles/journal_contribution/Construction_of_DNA_Tools_for_Hyperexpression_in_i_Marchantia_i_Chloroplasts/14744354Test

الإتاحة: https://doi.org/10.1021/acssynbio.0c00637.s001Test

المؤلفون: Chen Liu, Andriani Mentzelopoulou, Fotini Papagavriil, Prashanth Ramachandran, Artemis Perraki, Lucas Claus, Sebastian Barg, Peter Dörmann, Yvon Jaillais, Philipp Johnen, Eugenia Russinova, Electra Gizeli, Gabriel Schaaf, Panagiotis Nikolaou Moschou

الوصف: Protein function can be modulated by phase transitions in their material properties, which can range from liquid-to solid-like; yet the mechanisms that drive these transitions and whether they are important for physiology are still unknown. Using the model plant Arabidopsis, we show that developmental robustness is reinforced by phase transitions of the plasma membrane–bound lipid-binding protein SEC14-like. Using imaging, genetics, andin vitroreconstitution experiments, we show that SEC14-like undergoes liquid-like phase separation in the root stem cells. Outside the stem cell niche, SEC14-like associates with the caspase-like protease separase and conserved microtubule motors at unique polar plasma membrane interfaces. In these interfaces, SEC14-like undergoes abrupt processing by separase, which promotes its liquid-to-solid transition. The SEC14-like liquid-to-solid transition is important for root developmental robustness, as lines expressing an uncleavable SEC14-like variant or mutants of separase, and associated microtubule motors show similar developmental phenotypes. Furthermore, the processed and solidified but not the liquid form of SEC14-like interacts with the polar protein PINFORMED2 at the plasma membrane and perhaps other polar proteins of the PINFORMED family. This work demonstrates that robust development can involve abrupt liquid-to-solid transitions mediated by proteolysis at unique plasma membrane interfaces.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::d7f4e0e7250edeca1ae087bc3cb14fceTest
https://doi.org/10.1101/2022.03.26.485938Test

المؤلفون: Fernando Guzmán-Chávez, Harald Schneider, Eftychios Frangedakis, Jim Haseloff, Yang Liu, Susanna Sauret-Güeto, Artemis Perraki, Bernard Goffinet, Ying Yu, Marius Rebmann, Sze Wai Tse, Kasey Markel, Jenna Rever

المساهمون: Frangedakis, Eftychios [0000-0002-3483-8464], Rebmann, Marius [0000-0003-1462-0975], Markel, Kasey [0000-0002-8285-3888], Sauret-Gueto, Susanna [0000-0003-3792-8278], Haseloff, Jim [0000-0003-4793-8058], Apollo - University of Cambridge Repository

المصدر: ACS Synthetic Biology

مصطلحات موضوعية: 0106 biological sciences, Chloroplasts, Transcription, Genetic, Biomedical Engineering, DNA, Recombinant, plant, Genes, Plant, 01 natural sciences, Biochemistry, Genetics and Molecular Biology (miscellaneous), 03 medical and health sciences, Marchantia polymorpha, Transformation, Genetic, chloroplast, 010608 biotechnology, Marchantia, Plastid, 030304 developmental biology, Plant Proteins, 0303 health sciences, Reporter gene, biology, food and beverages, General Medicine, MRNA stabilization, biology.organism_classification, plastome, Cell biology, Chloroplast, Chloroplast DNA, Pentatricopeptide repeat, Synthetic Biology, Transcriptome, gene assembly, Research Article, Protein Binding

الوصف: Chloroplasts are attractive platforms for synthetic biology applications since they are capable of driving very high levels of transgene expression, if mRNA production and stability are properly regulated. However, plastid transformation is a slow process and currently limited to a few plant species. The liverwort Marchantia polymorpha is a simple model plant that allows rapid transformation studies; however, its potential for protein hyperexpression has not been fully exploited. This is partially due to the fact that chloroplast post-transcriptional regulation is poorly characterized in this plant. We have mapped patterns of transcription in Marchantia chloroplasts. Furthermore, we have obtained and compared sequences from 51 bryophyte species and identified putative sites for pentatricopeptide repeat protein binding that are thought to play important roles in mRNA stabilization. Candidate binding sites were tested for their ability to confer high levels of reporter gene expression in Marchantia chloroplasts, and levels of protein production and effects on growth were measured in homoplastic transformed plants. We have produced novel DNA tools for protein hyperexpression in this facile plant system that is a test-bed for chloroplast engineering.

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::770081f25359a8542ad7c1c3ad8d94ccTest
https://www.repository.cam.ac.uk/handle/1810/324776Test

المؤلفون: Xiyu Ma, Maricris Zaidem, Rainer Hedrich, Libo Shan, Andrea A. Gust, Artemis Perraki, Wei Lin Wan, Guido Grossmann, Rik Brugman, Jan A. L. van Kan, Lisha Zhang, Joachim Kilian, Elzbieta Krol, Mark Stahl, Cyril Zipfel, Rory N Pruitt, Detlef Weigel, Thorsten Nürnberger

المساهمون: University of Zurich, Gust, Andrea A

المصدر: New Phytologist, 221(4), 2080-2095
The New Phytologist
New Phytologist 221 (2019) 4

مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, Transcription, Genetic, Physiology, Arabidopsis, Plant Science, Immune receptor, 580 Plants (Botany), Cytoplasmic receptor, 01 natural sciences, 10126 Department of Plant and Microbial Biology, Plant Growth Regulators, 1110 Plant Science, receptor kinase, Phosphorylation, Receptor, receptor protein, biology, Full Paper, Pattern recognition receptor, Full Papers, Cell biology, Receptors, Pattern Recognition, plant immunity, Salicylic Acid, Sesquiterpenes, Signal Transduction, Genotype, chemical and pharmacologic phenomena, Protein Serine-Threonine Kinases, 03 medical and health sciences, Immune system, Phytoalexins, 10211 Zurich-Basel Plant Science Center, Kinase activity, Innate immune system, immune receptor, Arabidopsis Proteins, Research, fungi, 1314 Physiology, biology.organism_classification, Laboratorium voor Phytopathologie, 030104 developmental biology, Laboratory of Phytopathology, immune signaling comparison, EPS, Peptides, Reactive Oxygen Species, Protein Kinases, 010606 plant biology & botany, Flagellin

الوصف: Summary Pattern recognition receptors (PRRs) sense microbial patterns and activate innate immunity against attempted microbial invasions. The leucine‐rich repeat receptor kinases (LRR‐RK) FLS2 and EFR, and the LRR receptor protein (LRR‐RP) receptors RLP23 and RLP42, respectively, represent prototypical members of these two prominent and closely related PRR families.We conducted a survey of Arabidopsis thaliana immune signaling mediated by these receptors to address the question of commonalities and differences between LRR‐RK and LRR‐RP signaling.Quantitative differences in timing and amplitude were observed for several early immune responses, with RP‐mediated responses typically being slower and more prolonged than those mediated by RKs. Activation of RLP23, but not FLS2, induced the production of camalexin. Transcriptomic analysis revealed that RLP23‐regulated genes represent only a fraction of those genes differentially expressed upon FLS2 activation. Several positive and negative regulators of FLS2‐signaling play similar roles in RLP23 signaling. Intriguingly, the cytoplasmic receptor kinase BIK1, a positive regulator of RK signaling, acts as a negative regulator of RP‐type immune receptors in a manner dependent on BIK1 kinase activity.Our study unveiled unexpected differences in two closely related receptor systems and reports a new negative role of BIK1 in plant immunity.

وصف الملف: application/octet-stream; application/pdf; Wan_et_al-2019-New_Phytologist.pdf - application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a4febd76b681d40abf1d335d5151f23Test
https://doi.org/10.1111/nph.15497Test

المؤلفون: Susanna Sauret-Güeto, Bernard Goffinet, Ying Yu, Artemis Perraki, Yang Liu, Eftychios Frangedakis, Marius Rebmann, Fernando Guzmán-Chávez, Jenna Rever, Kasey Markel, Harald Schneider, Sze Wai Tse, Jim Haseloff

مصطلحات موضوعية: Chloroplast, Reporter gene, Marchantia polymorpha, biology, Gene expression, Marchantia, food and beverages, Pentatricopeptide repeat, Plastid, biology.organism_classification, Gene, Cell biology

الوصف: Chloroplast genes are present at high ploidy in plants, and capable of driving very high levels of gene expression if mRNA production and stability are properly regulated. Marchantia polymorpha is a simple model plant that allows rapid transformation studies, however post-transcriptional regulation in plastids is poorly characterized in this liverwort. We have mapped patterns of transcription in Marchantia chloroplasts. Furthermore, we have obtained and compared sequences from 51 early-divergent plant species, and identified putative sites for pentatricopeptide repeat protein binding that are thought to play important roles in mRNA stabilisation. Candidate binding sites were tested for their ability to confer high levels of reporter gene expression in Marchantia chloroplasts, and levels of protein production and effects on growth were measured in homoplasmic transformed plants. We have produced novel DNA tools for protein hyper-expression in a facile plant system that is a test-bed for chloroplast engineering.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::8c5147c6bb7f79eb2298b88f6ff9aa84Test
https://doi.org/10.1101/2020.11.27.401802Test

المؤلفون: Birgit Habenstein, Anthony Legrand, Julien Gronnier, Marie-Dominique Jolivet, Paul Gouguet, Anne-Flore Deroubaix, Sylvie German-Retana, Sébastien Mongrand, Marie Boudsocq, Artemis Perraki, Véronique Germain

المساهمون: Laboratoire de biogenèse membranaire (LBM), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), University of Tübingen, Department of Plant and Microbial Biology [Zurich, Suisse], Universität Zürich [Zürich] = University of Zurich (UZH), Chimie et Biologie des Membranes et des Nanoobjets (CBMN), École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Department of Plant Sciences, University of Cambridge, Cambridge, UK, Biologie du fruit et pathologie (BFP), Université de Bordeaux (UB)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut des Sciences des Plantes de Paris-Saclay (IPS2 (UMR_9213 / UMR_1403)), Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), French Ministère de l’Enseignement Supérieur et de la Recherche (MESR). EMBO LTF 438-2018 and ERC-2017-COG IMMUNO-PEPTALK ID: 773153. CNRS Momentum., ANR-19-CE13-0021,PhosphoREM-domain,Régulation de la communication intercellulaire - le rôle de la phosphoprotéine REMORIN liée aux nanodomaines de la membrane plasmique(2019), ANR-16-CE20-0008,PotyMove,Facteurs cellulaires recrutés par les potyvirus pour leur transport intercellulaire : de nouvelles sources de résistance des plantes?(2016), ANR-10-LABX-0040,SPS,Saclay Plant Sciences(2010), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), University of Cambridge [UK] (CAM), Université d'Évry-Val-d'Essonne (UEVE)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)

المصدر: Plant Physiol
Plant Physiology
Plant Physiology, American Society of Plant Biologists, 2021, 185 (3), pp.632-649. ⟨10.1093/plphys/kiaa063⟩
Plant Physiology, 2021, 185 (3), pp.632-649. ⟨10.1093/plphys/kiaa063⟩

مصطلحات موضوعية: 0106 biological sciences, Remorins, Protein family, Physiology, [SDV]Life Sciences [q-bio], Arabidopsis, Pathologie végétale, Plant Science, Computational biology, Biology, 01 natural sciences, 03 medical and health sciences, Membrane Microdomains, santé des plantes, mental disorders, Genetics, Focus Issue on Dynamic Membranes, Hormone signaling, 030304 developmental biology, Plant Proteins, 0303 health sciences, Interaction plante pathogène, Arabidopsis Proteins, musculoskeletal, neural, and ocular physiology, Cell Membrane, [SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacy, Phosphorylation, virologie végétale, psychological phenomena and processes, 010606 plant biology & botany

الوصف: REMORINs (REMs) are a plant-specific protein family, proposed regulators of membrane-associated molecular assemblies and well-established markers of plasma membrane nanodomains. REMs play a diverse set of functions in plant interactions with pathogens and symbionts, responses to abiotic stresses, hormone signaling and cell-to-cell communication. In this review, we highlight the established and more putative roles of REMs throughout the literature. We discuss the physiological functions of REMs, the mechanisms underlying their nanodomain-organization and their putative role as regulators of nanodomain-associated molecular assemblies. Furthermore, we discuss how REM phosphorylation may regulate their functional versatility. Overall, through data-mining and comparative analysis of the literature, we suggest how to further study the molecular mechanisms underpinning the functions of REMs.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b2f50feed6731ffe327335c95749e3eTest
https://pubmed.ncbi.nlm.nih.gov/33793872Test

المؤلفون: Paul Derbyshire, Daniel Couto, David Séré, Julian Avila, Xingyun Qi, Benjamin Schwessinger, Alberto P. Macho, Keiko U. Torii, Frank L.H. Menke, Lena Stransfeld, Artemis Perraki, Yasuhiro Kadota, Jan Sklenar, Cyril Zipfel, Thomas A. DeFalco, Shushu Jiang

المساهمون: Dept Plant Sci, University of Cambridge [UK] (CAM), Norwich Research Park, The Sainsbury Laboratory [Norwich] (TSL), Universität Zürich [Zürich] = University of Zurich (UZH), Sainsbury Lab, University of Washington [Seattle], Broad Institute of Harvard and MIT, Partenaires INRAE, 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), Research School of Biology, Australian National University (ANU), RIKEN Center for Sustainable Resource Science [Yokohama] (RIKEN CSRS), RIKEN - Institute of Physical and Chemical Research [Japon] (RIKEN), Shanghai Center for Plant Stress Biology, Chinese Academy of Sciences, Shanghai Institute for Biological Sciences, CAS, University of Geneva, Gatsby Charitable Foundation, European Research Council (grant 'PHOSPHinnATE'), Gordon and Betty Moore Foundation [GBMF3035], Howard Hughes Medical Institute, European Molecular Biology Organization (EMBO-LTFs) [100-2017, 225-2015], RIKEN Special Postdoctoral Research Fellowship, JSPS Excellent Young Researcher Overseas Visit Program, Uehara Memorial Foundation, JIC/TSL PhD Rotation Program, University of Zurich, Zipfel, Cyril

المصدر: Nature
Nature, Nature Publishing Group, 2018, 561 (7722), pp.248-252. ⟨10.1038/s41586-018-0471-x⟩

مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, Co-receptor, [SDV]Life Sciences [q-bio], 580 Plants (Botany), 01 natural sciences, Article, 03 medical and health sciences, 10126 Department of Plant and Microbial Biology, Arabidopsis, Arabidopsis thaliana, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, 10211 Zurich-Basel Plant Science Center, Tyrosine, 1000 Multidisciplinary, Multidisciplinary, biology, Kinase, fungi, Phosphoproteomics, biology.organism_classification, Cell biology, 030104 developmental biology, Phosphorylation, Function (biology), 010606 plant biology & botany

الوصف: International audience; Multicellular organisms use cell-surface receptor kinases to sense and process extracellular signals. Many plant receptor kinases are activated by the formation of ligand-induced complexes with shape-complementary co-receptors(1). The best-characterized co-receptor is BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1), which associates with numerous leucine-rich repeat receptor kinases (LRR-RKs) to control immunity, growth and development(2). Here we report key regulatory events that control the function of BAK1 and, more generally, LRR-RKs. Through a combination of phosphoproteomics and targeted mutagenesis, we identified conserved phosphosites that are required for the immune function of BAK1 in Arabidopsis thaliana. Notably, these phosphosites are not required for BAK1-dependent brassinosteroid-regulated growth. In addition to revealing a critical role for the phosphorylation of the BAK1 C-terminal tail, we identified a conserved tyrosine phosphosite that may be required for the function of the majority of Arabidopsis LRR-RKs, and which separates them into two distinct functional classes based on the presence or absence of this tyrosine. Our results suggest a phosphocode-based dichotomy of BAK1 function in plant signalling, and provide insights into receptor kinase activation that have broad implications for our understanding of how plants respond to their changing environment.

وصف الملف: s41586-018-0471-x.pdf - application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1ef63ba6e72a94f458fca95724369aeTest
https://hal.inrae.fr/hal-02627709Test