Characterization of Lipid Rafts from <i>Medicago truncatula</i> Root Plasma Membranes: A Proteomic Study Reveals the Presence of a Raft-Associated Redox System

Lefebvre, Benoît; Furt, Fabienne; Hartmann, Marie-Andrée; Michaelson, Louise V.; Carde, Jean‐Pierre; Sargueil-Boiron, Françoise; Rossignol, Michel; Napier, Johnathan A.; Cullimore, Julie V.; Bessoule, Jean‐Jacques; Mongrand, Sébastien

doi:10.1104/pp.106.094102

Cited by 240 publications

(233 citation statements)

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“…Association of the cytochrome here identified as AIR12 to the PM was previously demonstrated by analytical Suc gradient centrifugation of plant microsomes (Preger et al, 2005). This result is supplemented by recent proteomic studies that identified AIR12 as a PM protein (Dunkley et al, 2006) bound to the external face of the PM by means of a GPI anchor (Borner et al, 2003) and in association with lipid rafts (Lefebvre et al, 2007). AIR12 has been reported among secreted proteins of Medicago truncatula cell cultures, suggesting that the GPI anchor is cleaved under particular conditions with release of the protein (Kusumawati et al, 2008).…”

Section: Discussionsupporting

confidence: 56%

“…A DOMON-plus-cytochrome b561 protein (AC147406_ 8.1) has recently been detected in lipid rafts of M. truncatula roots together with AIR12 and other redox proteins (Lefebvre et al, 2007;i.e. orthologs of SKU5 and FQR1).…”

Section: Discussionmentioning

confidence: 99%

“…The protein is glycosylated and hydrophilic and predicted to be associated in vivo with the external face of the PM by means of a glycosylphosphatidylinositol (GPI) anchor (Borner et al, 2003). AIR12 has been found to be associated with lipid rafts together with other redox proteins (Lefebvre et al, 2007), which may act as its partners in a possible electron link between apoplast and symplast.…”

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confidence: 99%

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Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

et al. 2009

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We report here on the identification of the major plasma membrane (PM) ascorbate-reducible b-type cytochrome of bean (Phaseolus vulgaris) and soybean (Glycine max) hypocotyls as orthologs of Arabidopsis (Arabidopsis thaliana) AIR12 (for auxin induced in root cultures). Soybean AIR12, which is glycosylated and glycosylphosphatidylinositol-anchored to the external side of the PM in vivo, was expressed in Pichia pastoris in a recombinant form, lacking the glycosylphosphatidylinositol modification signal and purified from the culture medium. Recombinant AIR12 is a soluble protein predicted to fold into a b-sandwich domain and belonging to the DOMON (for dopamine b-monooxygenase N terminus) domain superfamily. It is shown to be a b-type cytochrome with a symmetrical a-band at 561 nm, fully reduced by ascorbate, and fully oxidized by monodehydroascorbate radical. AIR12 is a high-potential cytochrome b showing a wide bimodal dependence from the redox potential between +80 mV and +300 mV. Optical absorption and electron paramagnetic resonance analysis indicate that AIR12 binds a single, highly axial low-spin heme, likely coordinated by methionine-91 and histidine-76, which are strongly conserved in AIR12 sequences. Phylogenetic analyses reveal that the auxin-responsive genes AIR12 represent a new family of PM b-type cytochromes specific to flowering plants. Circumstantial evidence suggests that AIR12 may interact with other redox partners within the PM to constitute a redox link between cytoplasm and apoplast.

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Section: Discussionsupporting

confidence: 56%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

et al. 2009

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“…html). Protein association with detergent-resistant membranes (DRM) was inferred from the DRM proteomes of M. truncatula roots either non-mycorrhizal (Lefebvre et al 2007;Guillier et al 2014) or mycorrhizal (Lemaître-Guillier, personal communication). Functional classification was performed according to the FunCat scheme (Ruepp et al 2004).…”

Section: Digital Immunoblotting and Protein Characterizationmentioning

confidence: 99%

“…The mechanisms by which the AM-responsive proteins may associate with the PM fraction were further analyzed using in silico prediction programs for alpha-helical TM regions, lipid modifications, and N-terminal signal sequence on the dataset listed in Table 1. Because proteins also can be recruited to lateral lipid patches that form detergent-resistant microdomains (DRM) within the membrane (Lefebvre et al 2007;Guillier et al 2014), we also searched the DRM proteomes of M. truncatula roots for the presence of AMresponsive proteins. Figure 4b shows that alpha-helix and palmitoylation were the prevalent candidate processes, as predicted for 78 and 58% of the 82 proteins, respectively.…”

Section: Analysis Of the Am-responsive Proteinsmentioning

confidence: 99%

The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis

Aloui¹,

Recorbet²,

Lemaître‐Guillier³

et al. 2017

Mycorrhiza

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In arbuscular mycorrhizal (AM) roots, the plasma membrane (PM) of the host plant is involved in all developmental stages of the symbiotic interaction, from initial recognition to intracellular accommodation of intra-radical hyphae and arbuscules. Although the role of the PM as the agent for cellular morphogenesis and nutrient exchange is especially accentuated in endosymbiosis, very little is known regarding the PM protein composition of mycorrhizal roots. To obtain a global overview at the proteome level of the host PM proteins as modified by symbiosis, we performed a comparative protein profiling of PM fractions from Medicago truncatula roots either inoculated or not with the AM fungus Rhizophagus irregularis. PM proteins were isolated from root microsomes using an optimized discontinuous sucrose gradient; their subsequent analysis by liquid chromatography followed by mass spectrometry (MS) identified 674 proteins. Cross-species sequence homology searches combined with MS-based quantification clearly confirmed enrichment in PM-associated proteins and depletion of major microsomal contaminants. Changes in protein amounts between the PM proteomes of mycorrhizal and non-mycorrhizal roots were monitored further by spectral counting. This workflow identified a set of 82 mycorrhiza-responsive proteins that provided insights into the plant PM response to mycorrhizal symbiosis. Among them, the association of one third of the mycorrhiza-responsive proteins with detergent-resistant membranes pointed at partitioning to PM microdomains. The PM-associated proteins responsive to mycorrhization also supported host plant control of sugar uptake to limit fungal colonization, and lipid turnover events in the PM fraction of symbiotic roots. Because of the depletion upon symbiosis of proteins mediating the replacement of phospholipids by phosphorus-free lipids in the plasmalemma, we propose a role of phosphate nutrition in the PM composition of mycorrhizal roots.

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Lipid Rafts

Perraki¹,

Mongrand²

2012

Encyclopedia of Life Sciences

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The knowledge about the structure of the biological membrane changed during the last 70 years. In the 70s, Singer and Nicholson proposed the fluid mosaic model, a major conceptual breakthrough in which amphiphilic proteins reside within the lipid bilayer. In this dynamic structure, components can move laterally. Further works led to major modifications of this model. Indeed, functional aspects of trafficking and signal transduction suggested that lipids and proteins do not distribute randomly but can be sequestered in small domains, thus enhancing protein–protein interactions and speeding up signal transduction and enzyme activity. The ‘raft hypothesis’ was born. Rafts are small and transient microdomains enriched in sphingolipids and sterols, together with specific proteins with important functions. This hypothesis explains the heterogeneity of the distribution of membrane proteins by a spontaneous demixing of lipids to form domains involved in signal transduction, cell trafficking and host–pathogen relationship. Key Concepts: Biological membranes are organised in small, dynamic and transient domains called lipid rafts. Lipid rafts exist in all eukaryotic cells, mostly in the plasma membrane. Lipid rafts are enriched in sphingolipids and sterols, and depleted in phosphoglycerolipids. Lipid rafts are involved in signal transduction pathways, cell trafficking and host–pathogen relationship.

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Characterization of Lipid Rafts from Medicago truncatula Root Plasma Membranes: A Proteomic Study Reveals the Presence of a Raft-Associated Redox System

Cited by 240 publications

References 79 publications

Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

Auxin-Responsive Genes AIR12 Code for a New Family of Plasma Membrane b-Type Cytochromes Specific to Flowering Plants

The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis

Lipid Rafts

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