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Статті в журналах з теми "REMORINEs"
Cheng, Yan Wei, Ai Qing Feng, Zhen Bo Zhang, Yan Zhao Zhang, and Jian Ming Han. "The Phylogenetic Analysis and Identification of a Novel Remorin Member from Rice(Oryza sativa L) by Proteomics under Salt Stress." Advanced Materials Research 1073-1076 (December 2014): 229–32. http://dx.doi.org/10.4028/www.scientific.net/amr.1073-1076.229.
Повний текст джерелаJarsch, Iris K., and Thomas Ott. "Perspectives on Remorin Proteins, Membrane Rafts, and Their Role During Plant–Microbe Interactions." Molecular Plant-Microbe Interactions® 24, no. 1 (January 2011): 7–12. http://dx.doi.org/10.1094/mpmi-07-10-0166.
Повний текст джерелаLefebvre, Benoit, Ton Timmers, Malick Mbengue, Sandra Moreau, Christine Hervé, Katalin Tóth, Joana Bittencourt-Silvestre, et al. "A remorin protein interacts with symbiotic receptors and regulates bacterial infection." Proceedings of the National Academy of Sciences 107, no. 5 (January 19, 2010): 2343–48. http://dx.doi.org/10.1073/pnas.0913320107.
Повний текст джерелаWang, Yingqi, Jiaqi Li, Mengyu Li, Yuntong Li, Zibo Zhao, Cong Li, and Jing Yue. "Genome-Wide Characterization of Remorin Genes in Terms of Their Evolution and Expression in Response to Hormone Signals and Abiotic Stresses in Foxtail Millet (Setaria italica)." Diversity 14, no. 9 (August 27, 2022): 711. http://dx.doi.org/10.3390/d14090711.
Повний текст джерелаTraeger, Jeremiah, Dehong Hu, Mengran Yang, Gary Stacey, and Galya Orr. "Super-Resolution Imaging of Plant Receptor-Like Kinases Uncovers Their Colocalization and Coordination with Nanometer Resolution." Membranes 13, no. 2 (January 21, 2023): 142. http://dx.doi.org/10.3390/membranes13020142.
Повний текст джерелаMa, Zhiming, Yanbiao Sun, Xinlu Zhu, Liang Yang, Xu Chen, and Yansong Miao. "Membrane nanodomains modulate formin condensation for actin remodeling in Arabidopsis innate immune responses." Plant Cell 34, no. 1 (November 2, 2021): 374–94. http://dx.doi.org/10.1093/plcell/koab261.
Повний текст джерелаMa, Tingting, Shuai Fu, Kun Wang, Yaqin Wang, Jianxiang Wu, and Xueping Zhou. "Palmitoylation Is Indispensable for Remorin to Restrict Tobacco Mosaic Virus Cell-to-Cell Movement in Nicotiana benthamiana." Viruses 14, no. 6 (June 17, 2022): 1324. http://dx.doi.org/10.3390/v14061324.
Повний текст джерелаMartinez, Denis, Anthony Legrand, Julien Gronnier, Marion Decossas, Paul Gouguet, Olivier Lambert, Mélanie Berbon, et al. "Coiled-coil oligomerization controls localization of the plasma membrane REMORINs." Journal of Structural Biology 206, no. 1 (April 2019): 12–19. http://dx.doi.org/10.1016/j.jsb.2018.02.003.
Повний текст джерелаYu, Yunqing. "Remorins: Essential Regulators in Plant-Microbe Interaction and Cell Death Induction." Plant Physiology 183, no. 2 (June 2020): 435–36. http://dx.doi.org/10.1104/pp.20.00490.
Повний текст джерелаRaffaele, Sylvain, Sébastien Mongrand, Pascal Gamas, Andreas Niebel, and Thomas Ott. "Genome-Wide Annotation of Remorins, a Plant-Specific Protein Family: Evolutionary and Functional Perspectives." Plant Physiology 145, no. 3 (November 2007): 593–600. http://dx.doi.org/10.1104/pp.107.108639.
Повний текст джерелаДисертації з теми "REMORINEs"
Gronnier, Julien. "Function of Plant Plasma Membrane Nanodomains : Study of Group 1 REMORINs during Plant-Virus Interactions." Electronic Thesis or Diss., Bordeaux, 2016. http://www.theses.fr/2016BORD0327.
Повний текст джерелаOrganization by compartmentalization is a general property of natural systems coordinating biological events in space and time. Over the past three decades, it has been demonstrated that multiple micrometric to nano-metric sub-compartments co-exist at a single membrane level. Such membrane organization seems critical for most all cell bioactivities and therefore critical for development and survival of potentially all living organisms. Plants respond to pathogens by activating highly regulated plasma membrane-bound signalling pathways. Plant plasma membrane (PM) displays a great diversity of compartments, but underlying functions and molecular mechanisms governing such organization are not well understood. To get insight in how and why plant PM is compartmentalized, we choose to study the plant PM nanodomain goup 1 REMORIN during the interaction between N. benthamiana and the Potato Virus X (PVX). Using a multidisciplinary approach we decipher a molecular mechanism involved in defining REMORIN PM domains localization. Making mutants we provide a functional link between REMORIN PM organization at single molecule level, its phosphostatus, regulation of plasmodesmata permeability and PVX cell-to-cell movement restriction. We then provide evidences that during N.benthamiana PVX sensing, PM organization appears critical for the modulation plant defence mechanisms and cell signaling. This study provides a unique mechanistic insight into how tight control of protein spatio-temporal organization at PM level is crucial to confer membrane domains identity and functionality
Deroubaix, Anne-Flore. "Rôle de la rémorine et des nanodomaines membranaires dans la signalisation de la réponse aux phytovirus." Thesis, Bordeaux, 2019. http://www.theses.fr/2019BORD0292.
Повний текст джерелаIn the battle against viruses, plants have evolved various defence mechanisms to protect themselves against pathogens. Membrane-bound plant proteins such as Remorin (REM) may restrict viral infection. REMs belong to a plant-specific multigene family, classified in six phylogenetic groups that are localized in plasma membrane nanodomains and for some of them in plasmodesmata. Our team previously showed that in tomato and Nicotiana benthamiana, overexpression of Solanum tuberosum group 1 isoform 3 (StREM1.3) limits the cell-to-cell spread of the potexvirus Potato virus X (PVX) without affecting viral replication. During my thesis, our data allowed to built a working model in which the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3 (AtCPK3) is able to interact with group 1 REM in vivo, phosphorylates the N-terminal domain of StREM1.3 and, finally, with the help of uncharacterized proteins lead to the restriction of PVX cell-to-cell movement in N.benthamiana. N.benthamiana is perfect for viral experimentation, but is allo-tetraploid, making it difficult for genetic studies. Because of CPKs have 34 isoforms with likely functional redundancy between them, we switched to another pathosystem using the genetic toolbox of Arabidopsis thaliana and a potexvirus species able to infect A. thaliana, the Plantago Asiatica Mosaic Virus (PlAMV). The objectives are 1/ to study the contribution of different REM clades in potexvirus intercellular movement; 2/ to understand which CPKs are involved in this process using REM and CPKs single and multiple mutants, as well as AtCPKs over-expressors; 3/ To study the contribution of Group 1 REM and CPK3 on systemic potexvirus movement. We previously showed that, like PVX, PlAMV local movement is restricted by StREM1.3 and AtCPK3 in N.benthamiana. We optimized the experimental conditions to track and compare GFP-tagged PlAMV in different Arabidopsis genetic backgrounds. By using this method, we were able to track both local virus cell-to-cell movement and systemic infection through the whole plant. Group 1 REM and CPK single and multiple knock out mutants, as well as CPK over-expressors wereused. Interestingly, we did not detect any difference in propagation compared with control on various CPKs KO, except in cpk3 mutant. Indeed, both in local and systemic, PlAMV propagation is enhanced on cpk3 mutant while CPK3 overexpressing lines display an opposite effect, demonstrating the great involvement of CPK3 in potexvirus propagation. Similarly, we demonstrate the redundancy of each isoform from group 1 REM on the restriction of the intercellular movement of PlAMV. Interestingly, REM promotes intercellular propagation of another viral genus, the potyvirus genus, suggesting that REM functions are not general for all genera. Globally, our results classify group 1 REM and CPK3 as antiviral defence protein both in local and systemic potexvirus infection, and suggest that REM function is viral genus dependent. This research will pave the way toward new host targets to fight phytovirus infection
Jarsch, Iris. "Remorin proteins in Arabidopsis thaliana." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-181479.
Повний текст джерелаLegrand, Anthony. "Anchoring mechanism of the plant protein remorin to membrane nanodomains." Thesis, Bordeaux, 2020. http://www.theses.fr/2020BORD0285.
Повний текст джерелаGroup 1 isoform 3 remorin from Solanum tuberosum (StREM1.3) is a membrane protein belonging to the multigenic family of plant proteins called remorins (REMs), involved in plant immunity, symbiosis, abiotic stress resistance and hormone signalling. REMs’ most well known feature is their ability to segregate into nanodomains at the plasma membrane’s (PM) inner leaflet. For StREM1.3, this is achieved by an interaction between two lysines of the remorin C-terminal anchor (RemCA) and negatively charged phosphatidylinositol 4-phosphate (PI4P). Thus, RemCA undergoes conformational changes and partially buries itself in the PM, resulting in an intrinsic membrane anchoring. Capitalising on pre-existing structural data about this isoform, we investigate StREM1.3’s membrane-interacting properties further, using a wide array of techniques, ranging from fluorescence microscopy and solid-state nuclear magnetic resonance (ssNMR) to atomic force microscopy (AFM), cryo-electron microscopy (cryoEM) and computational modelling. We aim to discover the impact of StREM1.3’s oligomerisation and phosphorylation on its membrane interactions and biological activity, and to assess its influence on lipid dynamics as well as its lipid requirements for membrane binding and nanoclustering. Finally, based on all available structural data, we will undertake the in vitro reconstruction and characterisation of minimal nanodomains of StREM1.3
Popp, Claudia [Verfasser], and Thomas [Akademischer Betreuer] Ott. "Analysis of the membrane binding mechanism of Remorins and their role in beneficial endosymbioses / Claudia Popp ; Betreuer: Thomas Ott." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2017. http://d-nb.info/1137466820/34.
Повний текст джерелаGouguet, Paul. "Deciphering the proteic partners of REMORIN, a membrane-raft phosphoprotein implicated in plant cell-to-cell communication." Thesis, Bordeaux, 2018. http://www.theses.fr/2018BORD0418.
Повний текст джерелаGroup 1 REMORINs are plant-specific proteins located at the plasma membrane. We have shown that StREM1.3 (REM) is a marker of lipid rafts, plasma membrane domains enriched in sterols and sphingolipids. In addition, REM is enriched in plasmodesmata channels (PD) which are anchored within the cell wall and enable intercellular communication between virtually all plant cells. We have demonstrated for the first time the physiological role of REM in plants, this protein is able to reduce the viral cell-to-cell movement of Potato Virus X (PVX) and other viruses. Moreover, the antiviral activity of REM is regulated by phosphorylation and leads to a modification of the pore size of PD via the accumulation of callose, a sugar polymer, around the neck regions of PD. In order to understand how REM is able to induce the accumulation of callose in these specific regions, a large set of proteins have been selected and the deciphering of their functions have been initiated in planta by transgenic approaches, in transient expression and on transgenic plants, which will be subjected to viral infections to study the spread of viruses. Protein interaction, biochemistry and imaging approaches were also used to study this question. This thesis aims at understanding the mechanisms of the REM interaction with its membrane partners during viral infection, focusing on the protein-protein interactions during the response to PVX. We will focus more particularly on PD proteins and membrane rafts that are most likely targeted during this interaction with viruses
Konrad, Sebastian [Verfasser], and Thomas [Akademischer Betreuer] Ott. "The plasma membrane attachment of Remorin microdomain marker proteins is stabilized by S-acylation / Sebastian Konrad ; Betreuer: Thomas Ott." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2015. http://d-nb.info/1119706033/34.
Повний текст джерелаResta, Brenda. "Il processo di gestione informativa BIM per il progetto di un ponte in c.a.p.: la modellazione digitale del ponte Remorino a Minusio (Svizzera)." Master's thesis, Alma Mater Studiorum - Università di Bologna, 2021. http://amslaurea.unibo.it/24176/.
Повний текст джерелаJarsch, Iris Katharina [Verfasser], and Thomas [Akademischer Betreuer] Ott. "Remorin proteins in Arabidopsis thaliana : markers for diverse embrane micro-domains with roles in plant-microbe interactions / Iris Jarsch. Betreuer: Thomas Ott." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2014. http://d-nb.info/1072038250/34.
Повний текст джерелаMbengue, Malick. "Perception et transduction du signal bactérien facteur Nod dans l'établissement de la symbiose rhizobium-légumineuse : recherche et caractérisation de partenaires du LysM-RLK LYK3, un récepteur putatif des facteurs Nod chez Medicago truncatula." Toulouse 3, 2010. http://thesesups.ups-tlse.fr/1263/.
Повний текст джерелаLeguminous plants can establish symbiotic interaction with nitrogen fixing soil-born bacteria collectively referred as rhizobia. Nod factors (NFs) are rhizobia produced molecules essential to the establishment of this interaction. Genetic studies of the NFs perception in M. Truncatula led to the identification of two LysM receptor-like kinases, NFP and LYK3. NFP is necessary for all NFs induced responses while LYK3 specifically controls infection. Signalling events downstream LYK3 are poorly understood. To decipher this signalling pathway, two different yeast two-hybrid screens using M. Truncatula cDNAs and LYK3 kinase as bait were performed. One screen identified an E3 ubiquitin ligase of the U-Box family renamed MtPUB1. MtPUB1 plays a negative role in infection and nodulation, and as for LYK3, this role relies on the NFs structure produced by the rhizobia. In parallel, a second approach based on pairwise interaction assays identified a remorin protein as partner of all three symbiotic receptor-like kinases, NFP, LYK3 and DMI2
Книги з теми "REMORINEs"
Cerri, Roberto. Renzo Remorini (1927-1998): Da operaio comunista della Piaggio di Pontedera a "cittadino del mondo". Pontedera (Pisa): Tagete, 2004.
Знайти повний текст джерелаRemories Awaken to Life. Miraj Publishing Group, 2000.
Знайти повний текст джерелаRemorino, Francesco, and Giulia Remorino. Life : from Broken to Clarity: Di Francesco Remorino. Independently Published, 2020.
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