An update on plant membrane rafts

Simon-Plas, Françoise; Perraki, Artemis; Bayer, Emmanuelle; Gerbeau-Pissot, Patricia; Mongrand, Sébastien

doi:10.1016/j.pbi.2011.08.003

Cited by 97 publications

(83 citation statements)

References 56 publications

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“…A role for dynamic PM compartmentalization in response to environmental signals has recently begun to emerge in plant cells (Zappel and Panstruga, 2008;Mongrand et al, 2010;Simon-Plas et al, 2011), following a concept previously proposed in animal cells (Simons and Sampaio, 2011). Recent studies have shown how several abscisic acid signaling components interact within nanodomains in response to this phytohormone (Demir et al, 2013), as well as how the S-acylation of the small G protein Rop6 (which conditions its dynamic association to DIMs) is a critical determinant of its role in the regulation of cell polarity (Sorek et al, 2011).…”

Section: Cryptogein Transiently Induces a Modification In Tobacco Celmentioning

confidence: 95%

“…The function of dynamic PM compartmentalization in the detection and transduction of environmental signals in plant cells has only recently begun to emerge, along with a crucial role for sterols in this organization (for review, see Zappel and Panstruga, 2008;Mongrand et al, 2010;Simon-Plas et al, 2011). These observations make it indispensable to align how the surface membrane of living cells might reorganize during signaling with the membrane raft hypothesis.…”

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Modification of Plasma Membrane Organization in Tobacco Cells Elicited by Cryptogein

et al. 2013

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Lipid mixtures within artificial membranes undergo a separation into liquid-disordered and liquid-ordered phases. However, the existence of this segregation into microscopic liquid-ordered phases has been difficult to prove in living cells, and the precise organization of the plasma membrane into such phases has not been elucidated in plant cells. We developed a multispectral confocal microscopy approach to generate ratiometric images of the plasma membrane surface of Bright Yellow 2 tobacco (Nicotiana tabacum) suspension cells labeled with an environment sensitive fluorescent probe. This allowed the in vivo characterization of the global level of order of this membrane, by which we could demonstrate that an increase in its proportion of ordered phases transiently occurred in the early steps of the signaling triggered by cryptogein and flagellin, two elicitors of plant defense reactions. The use of fluorescence recovery after photobleaching revealed an increase in plasma membrane fluidity induced by cryptogein, but not by flagellin. Moreover, we characterized the spatial distribution of liquid-ordered phases on the membrane of living plant cells and monitored their variations induced by cryptogein elicitation. We analyze these results in the context of plant defense signaling, discuss their meaning within the framework of the "membrane raft" hypothesis, and propose a new mechanism of signaling platform formation in response to elicitor treatment.

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Section: Cryptogein Transiently Induces a Modification In Tobacco Celmentioning

confidence: 95%

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confidence: 99%

Modification of Plasma Membrane Organization in Tobacco Cells Elicited by Cryptogein

et al. 2013

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“…The composition of membrane rafts also prevents solubilization by detergent at low temperature with nonionic detergent and allows the partial purification of rafts in so-called Detergent-Insoluble Membrane (DIM) fractions, which are supposedly biochemical counterparts of membrane rafts. Many signaling proteins are found in membrane rafts, supporting the hypothesis that they serve as key platforms for cellular signal transduction and cell-to-cell communication (Lingwood and Simons, 2010;Simon-Plas et al, 2011). For example, in human (Homo sapiens) cells, key soluble signaling components such as the Ser/Thr kinase Akt (protein kinase B) are recruited to membrane rafts where they activate signal transduction cascades (Lasserre et al, 2008).…”

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confidence: 89%

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

et al. 2012

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The formation of plasma membrane (PM) microdomains plays a crucial role in the regulation of membrane signaling and trafficking. Remorins are a plant-specific family of proteins organized in six phylogenetic groups, and Remorins of group 1 are among the few plant proteins known to specifically associate with membrane rafts. As such, they are valuable to understand the molecular bases for PM lateral organization in plants. However, little is known about the structural determinants underlying the specific association of group 1 Remorins with membrane rafts. We used a structure-function approach to identify a short C-terminal anchor (RemCA) indispensable and sufficient for tight direct binding of potato (Solanum tuberosum) REMORIN 1.3 (StREM1.3) to the PM. RemCA switches from unordered to a-helical structure in a nonpolar environment. Protein structure modeling indicates that RemCA folds into a tight hairpin of amphipathic helices. Consistently, mutations reducing RemCA amphipathy abolished StREM1.3 PM localization. Furthermore, RemCA directly binds to biological membranes in vitro, shows higher affinity for Detergent-Insoluble Membranes lipids, and targets yellow fluorescent protein to Detergent-Insoluble Membranes in vivo. Mutations in RemCA resulting in cytoplasmic StREM1.3 localization abolish StREM1.3 function in restricting potato virus X movement. The mechanisms described here provide new insights on the control and function of lateral segregation of plant PM.

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“…Flotillin domain proteins are lipid raft-associated. Lipid raft-microdomains on plant membranes are dynamic, sterol and lipid rich protein assemblies that serve as centers for membrane trafficking and signaling events as they interact with a range of different proteins (126,127). FLOT4 is up-regulated in a strongly nod-factor dependent manner during early symbiotic events and has been localized to the infection thread membrane and the plasma membrane in root nodules (125).…”

Section: Soybean Symbiosome Proteomementioning

confidence: 99%

Proteomic Analysis of the Soybean Symbiosome Identifies New Symbiotic Proteins*

Clarke

Loughlin

Gavrin

et al. 2015

Molecular & Cellular Proteomics

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Legumes form a symbiosis with rhizobia in which the plant provides an energy source to the rhizobia bacteria that it uses to fix atmospheric nitrogen. This nitrogen is provided to the legume plant, allowing it to grow without the addition of nitrogen fertilizer. As part of the symbiosis, the bacteria in the infected cells of a new root organ, the nodule, are surrounded by a plant-derived membrane, the symbiosome membrane, which becomes the interface between the symbionts. Fractions containing the symbiosome membrane (SM) and material from the lumen of the symbiosome (peribacteroid space or PBS) were isolated from soybean root nodules and analyzed using nongel proteomic techniques. Bicarbonate stripping and chloroform-methanol extraction of isolated SM were used to reduce complexity of the samples and enrich for hydrophobic integral membrane proteins. One hundred and ninety-seven proteins were identified as components of the SM, with an additional fifteen proteins identified from peripheral membrane and PBS protein fractions. Proteins involved in a range of cellular processes such as metabolism, protein folding and degradation, membrane trafficking, and solute transport were identified. These included a number of proteins previously localized to the SM, such as aquaglyceroporin nodulin 26, sulfate transporters, remorin, and Rab7 homologs. Among the proteome were a number of putative transporters for compounds such as sulfate, calcium, hydrogen ions, peptide/ dicarboxylate, and nitrate, as well as transporters for which the substrate is not easy to predict. Analysis of the promoter activity for six genes encoding putative SM proteins showed nodule specific expression, with five showing expression only in infected cells. Localization of two proteins was confirmed using GFP-fusion experiments. The data have been deposited to the ProteomeXchange with identifier PXD001132. This proteome will provide a rich resource for the study of the legumerhizobium symbiosis. Molecular & Cellular Proteomics

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An update on plant membrane rafts

Cited by 97 publications

References 56 publications

Modification of Plasma Membrane Organization in Tobacco Cells Elicited by Cryptogein

Modification of Plasma Membrane Organization in Tobacco Cells Elicited by Cryptogein

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

Proteomic Analysis of the Soybean Symbiosome Identifies New Symbiotic Proteins*

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