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Journal articles on the topic 'REMORINEs'

Author: Grafiati

Published: 23 March 2023

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1

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.

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Rice root proteomics research identified to a new remorin1 protein,named OsREM1,which significantly increased (approximately 1.7-fold) compared with control under salt stress by Two-dimensional electrophoresis. It is found that the protein molecular weight is 29 kD, isoelectric point is 4.54. The bioinformatics analysis showed that: (1) The protein contains 195 amino acids, whose theoretical molecular weight is 21.3 kD, whose theoretical isoelectric point is 5.06. There are some differences with the experimental results, which may be the result of post-translational modification, such as glycosylation, phosphorylation; (2) The different crop remorin protein sequence alignment analysis found that the same rate of the amino acids is more than 50%, indicated that remorins are highly conserved protein; (3) Phylogenetic analysis showed OsREM1 had a low sequence identity with potao and tomato REM1, which is the agreement with traditional classification.

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2

Jarsch, 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.

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Invasion of host cells by pathogenic or mutualistic microbes requires complex molecular dialogues that often determine host survival. Although several components of the underlying signaling cascades have recently been identified and characterized, our understanding of proteins that facilitate signal transduction or assemble signaling complexes is rather sparse. Our knowledge of plant-specific remorin proteins, annotated as proteins with unknown function, has recently advanced with respect to their involvement in host–microbe interactions. Current data demonstrating that a remorin protein restricts viral movement in tomato leaves and the importance of a symbiosis-specific remorin for bacterial infection of root nodules suggest that these proteins may serve such regulatory functions. Direct interactions of other remorins with a resistance protein in Arabidopsis thaliana, and differential phosphorylation upon perception of microbial-associated molecular patterns and during expression of bacterial effector proteins, strongly underline their roles in plant defense. Furthermore, the specific subcellular localization of remorins in plasma membrane microdomains now provides the opportunity to visualize membrane rafts in living plants cells. There, remorins may oligomerize and act as scaffold proteins during early signaling events. This review summarizes current knowledge of this protein family and the potential roles of remorins in membrane rafts.

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3

Lefebvre, 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.

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Remorin proteins have been hypothesized to play important roles during cellular signal transduction processes. Induction of some members of this multigene family has been reported during biotic interactions. However, no roles during host-bacteria interactions have been assigned to remorin proteins until now. We used root nodule symbiosis between Medicago truncatula and Sinorhizobium meliloti to study the roles of a remorin that is specifically induced during nodulation. Here we show that this oligomeric remorin protein attaches to the host plasma membrane surrounding the bacteria and controls infection and release of rhizobia into the host cytoplasm. It interacts with the core set of symbiotic receptors that are essential for perception of bacterial signaling molecules, and thus might represent a plant-specific scaffolding protein.

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4

Wang, 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.

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Remorin genes encode plant-specific and plasma-membrane-associated proteins that play important roles in several plant physiological processes and adaptations to environmental adaptations. However, little is known regarding the remorin gene family in foxtail millet (Setaria italica), a traditional drought-resistant crop that grows in China. In this study, 21 remorin genes in the foxtail millet genome were identified, renamed according to their chromosomal distribution, and classified into four main groups based on their phylogenetic relationships and structural features. Additionally, we found that SiREM gene family expansion was primarily because of whole- genome duplication and segmental duplication events. Evolutionary changes in the remorin family in Poaceae crops were clarified via synteny analyses. Gene expression analyses through RT-PCR and qRT-PCR indicated that SiREM genes influenced millet growth and development, particularly SiREM1, 4, 11, and 12. Concurrently, SiREM genes expression showed inconsistent response to phytohormone treatments and abiotic stresses, suggesting that they are regulated by different signaling pathways. This systematic reanalysis remorin gene family in the foxtail millet provides fundamental information about the biological functions associated with growth, development, and stress tolerance and evolutionary characteristics, thus helping in elucidating the molecular mechanism and improving the agricultural traits of this crop in the future.

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5

Traeger, 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.

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Plant cell signaling often relies on the cellular organization of receptor-like kinases (RLKs) within membrane nanodomains to enhance signaling specificity and efficiency. Thus, nanometer-scale quantitative analysis of spatial organizations of RLKs could provide new understanding of mechanisms underlying plant responses to environmental stress. Here, we used stochastic optical reconstruction fluorescence microscopy (STORM) to quantify the colocalization of the flagellin-sensitive-2 (FLS2) receptor and the nanodomain marker, remorin, within Arabidopsis thaliana root hair cells. We found that recovery of FLS2 and remorin in the plasma membrane, following ligand-induced internalization by bacterial-flagellin-peptide (flg22), reached ~85% of their original membrane density after ~90 min. The pairs colocalized at the membrane at greater frequencies, compared with simulated randomly distributed pairs, except for directly after recovery, suggesting initial uncoordinated recovery followed by remorin and FLS2 pairing in the membrane. The purinergic receptor, P2K1, colocalized with remorin at similar frequencies as FLS2, while FLS2 and P2K1 colocalization occurred at significantly lower frequencies, suggesting that these RLKs mostly occupy distinct nanodomains. The chitin elicitor receptor, CERK1, colocalized with FLS2 and remorin at much lower frequencies, suggesting little coordination between CERK1 and FLS2. These findings emphasize STORM’s capacity to observe distinct nanodomains and degrees of coordination between plant cell receptors, and their respective immune pathways.

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6

Ma, 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.

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Abstract The assembly of macromolecules on the plasma membrane concentrates cell surface biomolecules into nanometer- to micrometer-scale clusters (nano- or microdomains) that help the cell initiate or respond to signals. In plant–microbe interactions, the actin cytoskeleton undergoes rapid remodeling during pathogen-associated molecular pattern-triggered immunity (PTI). The nanoclustering of formin-actin nucleator proteins at the cell surface has been identified as underlying actin nucleation during plant innate immune responses. Here, we show that the condensation of nanodomain constituents and the self-assembly of remorin proteins enables this mechanism of controlling formin condensation and activity during innate immunity in Arabidopsis thaliana. Through intrinsically disordered region-mediated remorin oligomerization and formin interaction, remorin gradually recruits and condenses formins upon PTI activation in lipid bilayers, consequently increasing actin nucleation in a time-dependent manner postinfection. Such nanodomain- and remorin-mediated regulation of plant surface biomolecules is expected to be a general feature of plant innate immune responses that creates spatially separated biochemical compartments and fine tunes membrane physicochemical properties for transduction of immune signals in the host.

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7

Ma, 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.

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Remorin (REM) is a plant-specific plasma membrane-associated protein regulating plasmodesmata plasticity and restricting viral cell-to-cell movement. Here, we show that palmitoylation is broadly present in group 1 remorin proteins in Nicotiana benthamiana and is crucial for plasma membrane localization and accumulation. By screening the four members of N. benthamiana group 1 remorin proteins, we found that only NbREM1.5 could significantly hamper tobacco mosaic virus (TMV) cell-to-cell movement. We further showed that NbREM1.5 interacts with the movement protein of TMV in vivo and interferes with its function of expanding the plasmodesmata size exclusion limit. We also demonstrated that palmitoylation is indispensable for NbREM1.5 to hamper plasmodesmata permeability and inhibit TMV cell-to-cell movement.

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8

Martinez, 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.

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9

Yu, 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.

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10

Raffaele, 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.

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11

Thibivilliers, Sandra, Andrew Farmer, and Marc Libault. "Biological and Cellular Functions of the Microdomain-Associated FWL/CNR Protein Family in Plants." Plants 9, no. 3 (March 19, 2020): 377. http://dx.doi.org/10.3390/plants9030377.

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Membrane microdomains/nanodomains are sub-compartments of the plasma membrane enriched in sphingolipids and characterized by their unique protein composition. They play important roles in regulating plant development and plant-microbe interactions including mutualistic symbiotic interactions. Several protein families are associated with the microdomain fraction of biological membranes such as flotillins, prohibitins, and remorins. More recently, GmFWL1, a FWL/CNR protein exclusively expressed in the soybean nodule, was functionally characterized as a new microdomain-associated protein. Interestingly, GmFWL1 is homologous to the tomato FW2-2 protein, a major regulator of tomato fruit development. In this review, we summarize the knowledge gained about the biological, cellular, and physiological functions of members of the FWL/CNR family across various plant species. The role of the FWL/CNR proteins is also discussed within the scope of their evolution and transcriptional regulation.

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12

Bar-Sinai, Sefi, Eduard Belausov, Vikas Dwivedi, and Einat Sadot. "Collisions of Cortical Microtubules with Membrane Associated Myosin VIII Tail." Cells 11, no. 1 (January 3, 2022): 145. http://dx.doi.org/10.3390/cells11010145.

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The distribution of myosin VIII ATM1 tail in association with the plasma membrane is often observed in coordination with that of cortical microtubules (MTs). The prevailing hypothesis is that coordination between the organization of cortical MTs and proteins in the membrane results from the inhibition of free lateral diffusion of the proteins by barriers formed by MTs. Since the positioning of myosin VIII tail in the membrane is relatively stable, we ask: can it affect the organization of MTs? Myosin VIII ATM1 tail co-localized with remorin 6.6, the position of which in the plasma membrane is also relatively stable. Overexpression of myosin VIII ATM1 tail led to a larger fraction of MTs with a lower rate of orientation dispersion. In addition, collisions between MTs and cortical structures labeled by ATM1 tail or remorin 6.6 were observed. Collisions between EB1 labeled MTs and ATM1 tail clusters led to four possible outcomes: 1—Passage of MTs through the cluster; 2—Decreased elongation rate; 3—Disengagement from the membrane followed by a change in direction; and 4—retraction. EB1 tracks became straighter in the presence of ATM1 tail. Taken together, collisions of MTs with ATM1 tail labeled structures can contribute to their coordinated organization.

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13

Huang, Dingquan, Yanbiao Sun, Zhiming Ma, Meiyu Ke, Yong Cui, Zichen Chen, Chaofan Chen, et al. "Salicylic acid-mediated plasmodesmal closure via Remorin-dependent lipid organization." Proceedings of the National Academy of Sciences 116, no. 42 (October 1, 2019): 21274–84. http://dx.doi.org/10.1073/pnas.1911892116.

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Plasmodesmata (PD) are plant-specific membrane-lined channels that create cytoplasmic and membrane continuities between adjacent cells, thereby facilitating cell–cell communication and virus movement. Plant cells have evolved diverse mechanisms to regulate PD plasticity in response to numerous environmental stimuli. In particular, during defense against plant pathogens, the defense hormone, salicylic acid (SA), plays a crucial role in the regulation of PD permeability in a callose-dependent manner. Here, we uncover a mechanism by which plants restrict the spreading of virus and PD cargoes using SA signaling by increasing lipid order and closure of PD. We showed that exogenous SA application triggered the compartmentalization of lipid raft nanodomains through a modulation of the lipid raft-regulatory protein, Remorin (REM). Genetic studies, superresolution imaging, and transmission electron microscopy observation together demonstrated that Arabidopsis REM1.2 and REM1.3 are crucial for plasma membrane nanodomain assembly to control PD aperture and functionality. In addition, we also found that a 14-3-3 epsilon protein modulates REM clustering and membrane nanodomain compartmentalization through its direct interaction with REM proteins. This study unveils a molecular mechanism by which the key plant defense hormone, SA, triggers membrane lipid nanodomain reorganization, thereby regulating PD closure to impede virus spreading.

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14

Tóth, Katalin, Thomas F. Stratil, Esben B. Madsen, Juanying Ye, Claudia Popp, Meritxell Antolín-Llovera, Christina Grossmann, et al. "Functional Domain Analysis of the Remorin Protein LjSYMREM1 in Lotus japonicus." PLoS ONE 7, no. 1 (January 23, 2012): e30817. http://dx.doi.org/10.1371/journal.pone.0030817.

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15

Jamann, Tiffany M., Xingyu Luo, Laura Morales, Judith M. Kolkman, Chia-Lin Chung, and Rebecca J. Nelson. "A remorin gene is implicated in quantitative disease resistance in maize." Theoretical and Applied Genetics 129, no. 3 (February 5, 2016): 591–602. http://dx.doi.org/10.1007/s00122-015-2650-6.

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16

Li, S., X. Su, B. Zhang, Q. Huang, Z. Hu, and M. Lu. "Molecular cloning and functional analysis of the Populus deltoides remorin gene PdREM." Tree Physiology 33, no. 10 (September 26, 2013): 1111–21. http://dx.doi.org/10.1093/treephys/tpt072.

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17

AOYAMA, TAKAO, MIKA MATSUMOTO, KIMIKO NAKAYAMA, KATSUYOSHI NAKAJIMA, FUMINORI SHIBUYA, HAJIME KOTAKI, YASUFUMI SAWADA, and TATSUJI IGA. "Studies on Determining the Endotoxin Concentration in Inulin Injections and Method of Remoring Endotoxin." Japanese Journal of Hospital Pharmacy 23, no. 2 (1997): 108–14. http://dx.doi.org/10.5649/jjphcs1975.23.108.

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18

Zhang, Huilong, Chen Deng, Xia Wu, Jun Yao, Yanli Zhang, Yinan Zhang, Shurong Deng, et al. "Populus euphratica remorin 6.5 activates plasma membrane H+-ATPases to mediate salt tolerance." Tree Physiology 40, no. 6 (March 3, 2020): 731–45. http://dx.doi.org/10.1093/treephys/tpaa022.

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Abstract Remorins (REMs) play an important role in the ability of plants to adapt to adverse environments. PeREM6.5, a protein of the REM family in Populus euphratica (salt-resistant poplar), was induced by NaCl stress in callus, roots and leaves. We cloned the full-length PeREM6.5 from P. euphratica and transformed it into Escherichia coli and Arabidopsis thaliana. PeREM6.5 recombinant protein significantly increased the H+-ATPase hydrolytic activity and H+ transport activity in P. euphratica plasma membrane (PM) vesicles. Yeast two-hybrid assay showed that P. euphratica REM6.5 interacted with RPM1-interacting protein 4 (PeRIN4). Notably, the PeREM6.5-induced increase in PM H+-ATPase activity was enhanced by PeRIN4 recombinant protein. Overexpression of PeREM6.5 in Arabidopsis significantly improved salt tolerance in transgenic plants in terms of survival rate, root growth, electrolyte leakage and malondialdehyde content. Arabidopsis plants overexpressing PeREM6.5 retained high PM H+-ATPase activity in both in vivo and in vitro assays. PeREM6.5-transgenic plants had reduced accumulation of Na+ due to the Na+ extrusion promoted by the H+-ATPases. Moreover, the H+ pumps caused hyperpolarization of the PM, which reduced the K+ loss mediated by the depolarization-activated channels in the PM of salinized roots. Therefore, we conclude that PeREM6.5 regulated H+-ATPase activity in the PM, thus enhancing the plant capacity to maintain ionic homeostasis under salinity.

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19

O'Toole, Bruce. "Phylogeny of the species of the superfamily Echeneoidea (Perciformes: Carangoidei: Echeneidae, Rachycentridae, and Coryphaenidae), with an interpretation of echeneid hitchhiking behaviour." Canadian Journal of Zoology 80, no. 4 (April 1, 2002): 596–623. http://dx.doi.org/10.1139/z02-031.

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A phylogenetic analysis, based on 138 putatively informative characters, of the 11 species of the superfamily Echeneoidea (Echeneidae, Rachycentridae, and Coryphaenidae) resulted in a single most parsimonious tree. This tree strongly supports the monophyly of the superfamily with the following relationships: Coryphaenidae + (Rachycentridae + (Phtheirichthys lineatus + ((Echeneis naucrates + Echeneis neucratoides) + (Remora brachyptera + (Remora remora + (Remora australis + (Remora osteochir + Remora albescens))))))). One of the traditional subfamilies, Echeneiinae, and one of the traditional genera, Remora, were both found to be paraphyletic. A new classification of the family based on natural groupings eliminated the subfamilial designations and subsumed the genus Remorina under the genus Remora, rendering it monophyletic. An examination of the behavioural data resulted in the hypothesis of a gradual step-by-step development of "hitchhiking" behaviour from general schooling behaviour (outgroups) to attaching to a select few types of hosts in the pelagic environment (as exhibited by R. osteochir).

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20

Raffaele, Sylvain, Artemis Perraki, and Sébastien Mongrand. "The Remorin C-terminal Anchor was shaped by convergent evolution among membrane binding domains." Plant Signaling & Behavior 8, no. 3 (March 2013): e23207. http://dx.doi.org/10.4161/psb.23207.

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21

Liang, Pengbo, Thomas F. Stratil, Claudia Popp, Macarena Marín, Jessica Folgmann, Kirankumar S. Mysore, Jiangqi Wen, and Thomas Ott. "Symbiotic root infections in Medicago truncatula require remorin-mediated receptor stabilization in membrane nanodomains." Proceedings of the National Academy of Sciences 115, no. 20 (April 30, 2018): 5289–94. http://dx.doi.org/10.1073/pnas.1721868115.

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Plant cell infection is tightly controlled by cell surface receptor-like kinases (RLKs). Like other RLKs, the Medicago truncatula entry receptor LYK3 laterally segregates into membrane nanodomains in a stimulus-dependent manner. Although nanodomain localization arises as a generic feature of plant membrane proteins, the molecular mechanisms underlying such dynamic transitions and their functional relevance have remained poorly understood. Here we demonstrate that actin and the flotillin protein FLOT4 form the primary and indispensable core of a specific nanodomain. Infection-dependent induction of the remorin protein and secondary molecular scaffold SYMREM1 results in subsequent recruitment of ligand-activated LYK3 and its stabilization within these membrane subcompartments. Reciprocally, the majority of this LYK3 receptor pool is destabilized at the plasma membrane and undergoes rapid endocytosis in symrem1 mutants on rhizobial inoculation, resulting in premature abortion of host cell infections. These data reveal that receptor recruitment into nanodomains is indispensable for their function during host cell infection.

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22

Marín, Macarena, Veronika Thallmair, and Thomas Ott. "The Intrinsically Disordered N-terminal Region of AtREM1.3 Remorin Protein Mediates Protein-Protein Interactions." Journal of Biological Chemistry 287, no. 47 (October 1, 2012): 39982–91. http://dx.doi.org/10.1074/jbc.m112.414292.

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23

Checker, Vibha G., and Paramjit Khurana. "Molecular and functional characterization of mulberry EST encoding remorin (MiREM) involved in abiotic stress." Plant Cell Reports 32, no. 11 (August 14, 2013): 1729–41. http://dx.doi.org/10.1007/s00299-013-1483-5.

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24

Cai, Jianghua, Guozheng Qin, Tong Chen, and Shiping Tian. "The mode of action of remorin1 in regulating fruit ripening at transcriptional and post-transcriptional levels." New Phytologist 219, no. 4 (July 6, 2018): 1406–20. http://dx.doi.org/10.1111/nph.15264.

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25

Bariola, Pauline, Dorota Retelska, Andrzej Stasiak, Richard Kammerer, Andrew Fleming, Mohamed Hijri, Sabine Frank, and Edward Farmer. "Remorins form a novel family of coiled coil-forming oligomeric and filamentous proteins associated with apical, vascular and embryonic tissues in plants." Plant Molecular Biology 55, no. 4 (July 2004): 579–94. http://dx.doi.org/10.1007/s11103-004-1520-4.

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Badawi, Mohamed A., Zahra Agharbaoui, Muhammad Zayed, Qiang Li, Brook Byrns, Jitao Zou, D. Brian Fowler, Jean Danyluk, and Fathey Sarhan. "Genome‐Wide Identification and Characterization of the Wheat Remorin ( Ta REM) Family during Cold Acclimation." Plant Genome 12, no. 2 (June 2019): 180040. http://dx.doi.org/10.3835/plantgenome2018.06.0040.

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27

Raffaele, Sylvain, Emmanuelle Bayer, David Lafarge, Stéphanie Cluzet, Sylvie German Retana, Tamy Boubekeur, Nathalie Leborgne-Castel, et al. "Remorin, a Solanaceae Protein Resident in Membrane Rafts and Plasmodesmata, Impairs Potato virus X Movement." Plant Cell 21, no. 5 (May 2009): 1541–55. http://dx.doi.org/10.1105/tpc.108.064279.

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Cheng, Guangyuan, Zongtao Yang, Hai Zhang, Jisen Zhang, and Jingsheng Xu. "Remorin interacting with PCaP1 impairs Turnip mosaic virus intercellular movement but is antagonised by VPg." New Phytologist 225, no. 5 (November 21, 2019): 2122–39. http://dx.doi.org/10.1111/nph.16285.

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29

Son, Seungmin, Chang Jae Oh, and Chung Sun An. "Arabidopsis thaliana Remorins Interact with SnRK1 and Play a Role in Susceptibility to Beet Curly Top Virus and Beet Severe Curly Top Virus." Plant Pathology Journal 30, no. 3 (September 1, 2014): 269–78. http://dx.doi.org/10.5423/ppj.oa.06.2014.0061.

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Rocher, Marion, Vincent Simon, Marie-Dominique Jolivet, Luc Sofer, Anne-Flore Deroubaix, Véronique Germain, Sébastien Mongrand, and Sylvie German-Retana. "StREM1.3 REMORIN Protein Plays an Agonistic Role in Potyvirus Cell-to-Cell Movement in N. benthamiana." Viruses 14, no. 3 (March 10, 2022): 574. http://dx.doi.org/10.3390/v14030574.

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REMORIN proteins belong to a plant-specific multigene family that localise in plasma membrane nanodomains and in plasmodesmata. We previously showed that in Nicotiana benthamiana, group 1 StREM1.3 limits the cell-to-cell spread of a potexvirus without affecting viral replication. This prompted us to check whether an effect on viral propagation could apply to potyvirus species Turnip mosaic virus (TuMV) and Potato virus A (PVA). Our results show that StREM1.3 transient or stable overexpression in transgenic lines increases potyvirus propagation, while it is slowed down in transgenic lines underexpressing endogenous NbREMs, without affecting viral replication. TuMV and PVA infection do not alter the membranous localisation of StREM1.3. Furthermore, StREM1.3-membrane anchoring is necessary for its agonist effect on potyvirus propagation. StREM1.3 phosphocode seems to lead to distinct plant responses against potexvirus and potyvirus. We also showed that StREM1.3 interacts in yeast and in planta with the key potyviral movement protein CI (cylindrical inclusion) at the level of the plasma membrane but only partially at plasmodesmata pit fields. TuMV infection also counteracts StREM1.3-induced plasmodesmata callose accumulation at plasmodesmata. Altogether, these results showed that StREM1.3 plays an agonistic role in potyvirus cell-to-cell movement in N. benthamiana.

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Ovchinnikova, Evgenia, Etienne-Pascal Journet, Mireille Chabaud, Viviane Cosson, Pascal Ratet, Gerard Duc, Elena Fedorova, et al. "IPD3 Controls the Formation of Nitrogen-Fixing Symbiosomes in Pea and Medicago Spp." Molecular Plant-Microbe Interactions® 24, no. 11 (November 2011): 1333–44. http://dx.doi.org/10.1094/mpmi-01-11-0013.

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A successful nitrogen-fixing symbiosis requires the accommodation of rhizobial bacteria as new organelle-like structures, called symbiosomes, inside the cells of their legume hosts. Two legume mutants that are most strongly impaired in their ability to form symbiosomes are sym1/TE7 in Medicago truncatula and sym33 in Pisum sativum. We have cloned both MtSYM1 and PsSYM33 and show that both encode the recently identified interacting protein of DMI3 (IPD3), an ortholog of Lotus japonicus (Lotus) CYCLOPS. IPD3 and CYCLOPS were shown to interact with DMI3/CCaMK, which encodes a calcium- and calmodulin-dependent kinase that is an essential component of the common symbiotic signaling pathway for both rhizobial and mycorrhizal symbioses. Our data reveal a novel, key role for IPD3 in symbiosome formation and development. We show that MtIPD3 participates in but is not essential for infection thread formation and that MtIPD3 also affects DMI3-induced spontaneous nodule formation upstream of cytokinin signaling. Further, MtIPD3 appears to be required for the expression of a nodule-specific remorin, which controls proper infection thread growth and is essential for symbiosome formation.

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Gui, J., C. Liu, J. Shen, and L. Li. "Grain setting defect1, Encoding a Remorin Protein, Affects the Grain Setting in Rice through Regulating Plasmodesmatal Conductance." PLANT PHYSIOLOGY 166, no. 3 (September 24, 2014): 1463–78. http://dx.doi.org/10.1104/pp.114.246769.

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Son, Seungmin, Chang Jae Oh, Ju-Hee Bae, Hyoungseok Lee, and Chung Sun An. "GmREM1.1 and GmREM2.1, which encode the remorin proteins in soybean, have distinct roles during root nodule development." Journal of Plant Biology 58, no. 1 (January 15, 2015): 17–25. http://dx.doi.org/10.1007/s12374-014-0273-0.

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Kong, Chao-Yue, Yong-ping Luo, Ting-Ting Duan, Zhen Xue, Xiu-Dan Gao, Xin Zhao, and Gang Gao. "Potato remorin gene StREMa4 cloning and its spatiotemporal expression pattern under Ralstonia solanacearum and plant hormones treatment." Phytoparasitica 44, no. 4 (September 2016): 575–84. http://dx.doi.org/10.1007/s12600-016-0536-z.

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Tran, Tuan Minh, Choon-Peng Chng, Xiaoming Pu, Zhiming Ma, Xiao Han, Xiaolin Liu, Liang Yang, Changjin Huang, and Yansong Miao. "Potentiation of plant defense by bacterial outer membrane vesicles is mediated by membrane nanodomains." Plant Cell 34, no. 1 (November 13, 2021): 395–417. http://dx.doi.org/10.1093/plcell/koab276.

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Abstract Outer membrane vesicles (OMVs) are released from the outer membranes of Gram-negative bacteria during infection and modulate host immunity during host–pathogen interactions. The mechanisms by which OMVs are perceived by plants and affect host immunity are unclear. Here, we used the pathogen Xanthomonas campestris pv. campestris to demonstrate that OMV–plant interactions at the Arabidopsis thaliana plasma membrane (PM) modulate various host processes, including endocytosis, innate immune responses, and suppression of pathogenesis by phytobacteria. The lipid phase of OMVs is highly ordered and OMVs directly insert into the Arabidopsis PM, thereby enhancing the plant PM’s lipid order; this also resulted in strengthened plant defenses. Strikingly, the integration of OMVs into the plant PM is host nanodomain- and remorin-dependent. Using coarse-grained simulations of molecular dynamics, we demonstrated that OMV integration into the plant PM depends on the membrane lipid order. Our computational simulations further showed that the saturation level of the OMV lipids could fine-tune the enhancement of host lipid order. Our work unraveled the mechanisms underlying the ability of OMVs produced by a plant pathogen to insert into the host PM, alter host membrane properties, and modulate plant immune responses.

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Fu, Shuai, Yi Xu, Chenyang Li, Yi Li, Jianxiang Wu, and Xueping Zhou. "Rice Stripe Virus Interferes with S-acylation of Remorin and Induces Its Autophagic Degradation to Facilitate Virus Infection." Molecular Plant 11, no. 2 (February 2018): 269–87. http://dx.doi.org/10.1016/j.molp.2017.11.011.

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Konrad, Sebastian S. A., Claudia Popp, Thomas F. Stratil, Iris K. Jarsch, Veronika Thallmair, Jessica Folgmann, Macarena Marín, and Thomas Ott. "S-acylation anchors remorin proteins to the plasma membrane but does not primarily determine their localization in membrane microdomains." New Phytologist 203, no. 3 (June 4, 2014): 758–69. http://dx.doi.org/10.1111/nph.12867.

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Raffaele, Sylvain, Emmanuelle Bayer, and Sébastien Mongrand. "Up regulation of the plant protein remorin correlates with dehiscence and cell maturation; a link with the maturation of plasmodesmata?" Plant Signaling & Behavior 4, no. 10 (October 2009): 915–19. http://dx.doi.org/10.4161/psb.4.10.9661.

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Ke, Meiyu, Zhiming Ma, Deyan Wang, Yanbiao Sun, Chenjin Wen, Dingquan Huang, Zichen Chen, et al. "Salicylic acid regulates PIN2 auxin transporter hyperclustering and root gravitropic growth via Remorin ‐dependent lipid nanodomain organisation in Arabidopsis thaliana." New Phytologist 229, no. 2 (September 30, 2020): 963–78. http://dx.doi.org/10.1111/nph.16915.

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Torres, Gonzalo, Estrella Armada-Cortés, Javier Rueda, Alejandro F. San Juan, and Enrique Navarro. "Comparison of Hamstrings and Quadriceps Muscle Activation in Male and Female Professional Soccer Players." Applied Sciences 11, no. 2 (January 14, 2021): 738. http://dx.doi.org/10.3390/app11020738.

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(1) Background: this study aimed to determine if there are differences in quadriceps and hamstring muscle activation in professional male and female soccer players. (2) Methods: muscle activation was recorded by surface electromyography in 27 professional soccer players (19 male and 8 female). The players performed the Bulgarian squat and lunge exercises. Vastus medialis, vastus lateralis, rectus femoris, semitendinosus, and biceps femoris were the muscles analyzed. (3) Results: The statistical analysis of the hamstring:quadriceps ratio showed no significant differences (p > 0.05). Significant differences were found in the vastus medialis:vastus lateralis ratio for both the lunge exercise (t20 = 3.35; p = 0.001; d = 1.42) and the Bulgarian squat (t23 = 4.15; p < 0.001; d = 1.76). For the intragroup muscular pattern in the lunge and Bulgarian squat exercises, the female players showed higher activation for the vastus lateralis muscle (p < 0.001) than the male players and lower muscle activation in the vastus medialis. No significant differences were found in the rectus femoris, biceps remoris, and semitendinosus muscles (p > 0.05). (4) Conclusions: Differences were found in the medial ratio (vastus medialis: vastus lateralis). Moreover, regarding the intramuscular pattern, very consistent patterns have been found. In the quadriceps muscle: VM>VL>RF; in the hamstring muscle: ST>BF. These patterns could be very useful in the recovery process from an injury to return players to their highest performance.

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Khoza, Thembisile, Ian Dubery, and Lizelle Piater. "Identification of Candidate Ergosterol-Responsive Proteins Associated with the Plasma Membrane of Arabidopsis thaliana." International Journal of Molecular Sciences 20, no. 6 (March 14, 2019): 1302. http://dx.doi.org/10.3390/ijms20061302.

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The impact of fungal diseases on crop production negatively reflects on sustainable food production and overall economic health. Ergosterol is the major sterol component in fungal membranes and regarded as a general elicitor or microbe-associated molecular pattern (MAMP) molecule. Although plant responses to ergosterol have been reported, the perception mechanism is still unknown. Here, Arabidopsis thaliana protein fractions were used to identify those differentially regulated following ergosterol treatment; additionally, they were subjected to affinity-based chromatography enrichment strategies to capture and categorize ergosterol-interacting candidate proteins using liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS). Mature plants were treated with 250 nM ergosterol over a 24 h period, and plasma membrane-associated fractions were isolated. In addition, ergosterol was immobilized on two different affinity-based systems to capture interacting proteins/complexes. This resulted in the identification of defense-related proteins such as chitin elicitor receptor kinase (CERK), non-race specific disease resistance/harpin-induced (NDR1/HIN1)-like protein, Ras-related proteins, aquaporins, remorin protein, leucine-rich repeat (LRR)- receptor like kinases (RLKs), G-type lectin S-receptor-like serine/threonine-protein kinase (GsSRK), and glycosylphosphatidylinositol (GPI)-anchored protein. Furthermore, the results elucidated unknown signaling responses to this MAMP, including endocytosis, and other similarities to those previously reported for bacterial flagellin, lipopolysaccharides, and fungal chitin.

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Albers, Philip, Suayib Üstün, Katja Witzel, Max Kraner, and Frederik Börnke. "A Remorin from Nicotiana benthamiana Interacts with the Pseudomonas Type-III Effector Protein HopZ1a and is Phosphorylated by the Immune-Related Kinase PBS1." Molecular Plant-Microbe Interactions® 32, no. 9 (September 2019): 1229–42. http://dx.doi.org/10.1094/mpmi-04-19-0105-r.

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The plasma membrane (PM) is at the interface of plant–pathogen interactions and, thus, many bacterial type-III effector (T3E) proteins target membrane-associated processes to interfere with immunity. The Pseudomonas syringae T3E HopZ1a is a host cell PM-localized effector protein that has several immunity-associated host targets but also activates effector-triggered immunity in resistant backgrounds. Although HopZ1a has been shown to interfere with early defense signaling at the PM, no dedicated PM-associated HopZ1a target protein has been identified until now. Here, we show that HopZ1a interacts with the PM-associated remorin protein NbREM4 from Nicotiana benthamiana in several independent assays. NbREM4 relocalizes to membrane nanodomains after treatment with the bacterial elicitor flg22 and transient overexpression of NbREM4 in N. benthamiana induces the expression of a subset of defense-related genes. We can further show that NbREM4 interacts with the immune-related receptor-like cytoplasmic kinase avrPphB-susceptible 1 (PBS1) and is phosphorylated by PBS1 on several residues in vitro. Thus, we conclude that NbREM4 is associated with early defense signaling at the PM. The possible relevance of the HopZ1a–NbREM4 interaction for HopZ1a virulence and avirulence functions is discussed. [Formula: see text]Copyright © 2019 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license .

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Yue, Jing, Cong Li, Yuwei Liu, and Jingjuan Yu. "A Remorin Gene SiREM6, the Target Gene of SiARDP, from Foxtail Millet (Setaria italica) Promotes High Salt Tolerance in Transgenic Arabidopsis." PLoS ONE 9, no. 6 (June 26, 2014): e100772. http://dx.doi.org/10.1371/journal.pone.0100772.

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Bachmann, Herwig, Marjo J. C. Starrenburg, Annereinou Dijkstra, Douwe Molenaar, Michiel Kleerebezem, Jan L. W. Rademaker, and Johan E. T. van Hylckama Vlieg. "Regulatory Phenotyping Reveals Important Diversity within the Species Lactococcus lactis." Applied and Environmental Microbiology 75, no. 17 (July 10, 2009): 5687–94. http://dx.doi.org/10.1128/aem.00919-09.

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ABSTRACT The diversity in regulatory phenotypes among a collection of 84 Lactococcus lactis strains isolated from dairy and nondairy origin was explored. The specific activities of five enzymes were assessed in cell extracts of all strains grown in two different media, a nutritionally rich broth and a relatively poor chemically defined medium. The five investigated enzymes, branched chain aminotransferase (BcaT), aminopeptidase N (PepN), X-prolyl dipeptidyl peptidase (PepX), alpha-hydroxyisocaproic acid dehydrogenase (HicDH), and esterase, are involved in nitrogen and fatty acid metabolism and catalyze key steps in the production of important dairy flavor compounds. The investigated cultures comprise 75 L. lactis subsp. lactis isolates (including 7 L. lactis subsp. lactis biovar diacetylactis isolates) and 9 L. lactis subsp. c remoris isolates. All L. lactis subsp. cremoris and 22 L. lactis subsp. lactis (including 6 L. lactis subsp. lactis biovar diacetylactis) cultures originated from a dairy environment. All other cultures originated from (fermented) plant materials and were isolated at different geographic locations. Correlation analysis of specific enzyme activities revealed significantly different regulatory phenotypes for dairy and nondairy isolates. The enzyme activities in the two investigated media were in general poorly correlated and revealed a high degree of regulatory diversity within this collection of closely related strains. To the best of our knowledge, these results represent the most extensive diversity analysis of regulatory phenotypes within a single bacterial species to date. The presented findings underline the importance of the availability of screening procedures for, e.g., industrially relevant enzyme activities in models closely mimicking application conditions. Moreover, they corroborate the notion that regulatory changes are important drivers of evolution.

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Perraki, Artemis, Jean-Luc Cacas, Jean-Marc Crowet, Laurence Lins, Michel Castroviejo, Sylvie German-Retana, Sébastien Mongrand, and Sylvain Raffaele. "Plasma Membrane Localization of Solanum tuberosum Remorin from Group 1, Homolog 3 Is Mediated by Conformational Changes in a Novel C-Terminal Anchor and Required for the Restriction of Potato Virus X Movement]." Plant Physiology 160, no. 2 (August 1, 2012): 624–37. http://dx.doi.org/10.1104/pp.112.200519.

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Gronnier, Julien, Jean-Marc Crowet, Birgit Habenstein, Mehmet Nail Nasir, Vincent Bayle, Eric Hosy, Matthieu Pierre Platre, et al. "Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains." eLife 6 (July 31, 2017). http://dx.doi.org/10.7554/elife.26404.

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Plasma Membrane is the primary structure for adjusting to ever changing conditions. PM sub-compartmentalization in domains is thought to orchestrate signaling. Yet, mechanisms governing membrane organization are mostly uncharacterized. The plant-specific REMORINs are proteins regulating hormonal crosstalk and host invasion. REMs are the best-characterized nanodomain markers via an uncharacterized moiety called REMORIN C-terminal Anchor. By coupling biophysical methods, super-resolution microscopy and physiology, we decipher an original mechanism regulating the dynamic and organization of nanodomains. We showed that targeting of REMORIN is independent of the COP-II-dependent secretory pathway and mediated by PI4P and sterol. REM-CA is an unconventional lipid-binding motif that confers nanodomain organization. Analyses of REM-CA mutants by single particle tracking demonstrate that mobility and supramolecular organization are critical for immunity. This study provides a unique mechanistic insight into how the tight control of spatial segregation is critical in the definition of PM domain necessary to support biological function.

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Su, Chao, Marta Rodriguez-Franco, Beatrice Lace, Nils Nebel, Casandra Hernandez-Reyes, Pengbo Liang, Eija Schulze, et al. "Stabilization of membrane topologies by proteinaceous remorin scaffolds." Nature Communications 14, no. 1 (January 19, 2023). http://dx.doi.org/10.1038/s41467-023-35976-5.

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AbstractIn plants, the topological organization of membranes has mainly been attributed to the cell wall and the cytoskeleton. Additionally, few proteins, such as plant-specific remorins have been shown to function as protein and lipid organizers. Root nodule symbiosis requires continuous membrane re-arrangements, with bacteria being finally released from infection threads into membrane-confined symbiosomes. We found that mutations in the symbiosis-specific SYMREM1 gene result in highly disorganized perimicrobial membranes. AlphaFold modelling and biochemical analyses reveal that SYMREM1 oligomerizes into antiparallel dimers and may form a higher-order membrane scaffolding structure. This was experimentally confirmed when expressing this and other remorins in wall-less protoplasts is sufficient where they significantly alter and stabilize de novo membrane topologies ranging from membrane blebs to long membrane tubes with a central actin filament. Reciprocally, mechanically induced membrane indentations were equally stabilized by SYMREM1. Taken together we describe a plant-specific mechanism that allows the stabilization of large-scale membrane conformations independent of the cell wall.

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Farfán López, Edwin, Arturo Acero P., and Marcela Grijalba Bendeck. "OCCURRENCE OF REMORINA ALBESCENS (PERCIFORMES: ECHENEIDAE) IN THE COLOMBIAN CARIBBEAN, INCLUDING A TAXONOMIC KEY FOR SPECIES OF THE FAMILY IN COLOMBIA." Bulletin of Marine and Coastal Research 38, no. 2 (January 1, 2016). http://dx.doi.org/10.25268/bimc.invemar.2009.38.2.344.

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The presence of Remorina albescens for the Colombian Caribbean is conrmed, based on a specimen of 165.91 mm of standard length collected in Nenguanje bay at the Tayrona National Natural Park. A taxonomic key for the remoras known from Colombian seas is also included.

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Marín, Macarena, and Thomas Ott. "Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins." Frontiers in Plant Science 3 (2012). http://dx.doi.org/10.3389/fpls.2012.00086.

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Legrand, Anthony, Daniel G.-Cava, Marie-Dominique Jolivet, Marion Decossas, Olivier Lambert, Vincent Bayle, Yvon Jaillais, et al. "Structural determinants of REMORIN nanodomain formation in anionic membranes." Biophysical Journal, December 2022. http://dx.doi.org/10.1016/j.bpj.2022.12.035.

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