Cell wall proteins: a new insight through proteomics

Jamet, Élisabeth; Canut, Hervé; Boudart, Georges; Pont‐Lezica, Rafael

doi:10.1016/j.tplants.2005.11.006

Cited by 255 publications

(221 citation statements)

References 76 publications

(93 reference statements)

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“…The next closest paralog in the Arabidopsis genome is AtAGLU1, a putative a-glucosidase whose translation product has been located in the vacuole in several proteomic studies (Carter et al, 2004;Shimaoka et al, 2004). We have previously presented evidence of the cell wall location of Arabidopsis a-xylosidase activity (Sampedro et al, 2001), and numerous studies have identified AtXYL1 in the cell wall proteome (Jamet et al, 2006). It is thus likely that the only cell wall enzyme capable of removing Xyl residues from xyloglucan oligosaccharides is AtXYL1.…”

Section: Discussionmentioning

confidence: 99%

Lack of α-Xylosidase Activity in Arabidopsis Alters Xyloglucan Composition and Results in Growth Defects

et al. 2010

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Xyloglucan is the main hemicellulose in the primary cell walls of most seed plants and is thought to play a role in regulating the separation of cellulose microfibrils during growth. Xylose side chains block the degradation of the backbone, and a-xylosidase activity is necessary to remove them. Two Arabidopsis (Arabidopsis thaliana) mutant lines with insertions in the a-xylosidase gene AtXYL1 were characterized in this work. Both lines showed a reduction to undetectable levels of a-xylosidase activity against xyloglucan oligosaccharides. This reduction resulted in the accumulation of XXXG and XXLG in the liquid growth medium of Atxyl1 seedlings. The presence of XXLG suggests that it is a poor substrate for xyloglucan b-galactosidase. In addition, the polymeric xyloglucan of Atxyl1 lines was found to be enriched in XXLG subunits, with a concomitant decrease in XXFG and XLFG. This change can be explained by extensive exoglycosidase activity at the nonreducing ends of xyloglucan chains. These enzymes could thus have a larger role than previously thought in the metabolism of xyloglucan. Finally, Atxyl1 lines showed a reduced ability to control the anisotropic growth pattern of different organs, pointing to the importance of xyloglucan in this process. The promoter of AtXYL1 was shown to direct expression to many different organs and cell types undergoing cell wall modifications, including trichomes, vasculature, stomata, and elongating anther filaments.

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Section: Discussionmentioning

confidence: 99%

Lack of α-Xylosidase Activity in Arabidopsis Alters Xyloglucan Composition and Results in Growth Defects

et al. 2010

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“…For physical and biological reasons including interactions of the plasmalemma with other organelles such as the cell wall and the endoplasmic reticulum (Jamet et al 2006;Quon and Beh 2015), organelles cannot be isolated to absolute purity. Consequently, both the enrichment in plasmalemmic proteins and depletion of contaminants also needs to be quantified by comparing protein abundances in crude and purified fractions (Yadeta et al 2013).…”

Section: Purity Of Root Pm Fractionsmentioning

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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“…Analyses of protein populations from the walls of many plant organs and tissues have been reported (for review, see Lee et al, 2004;Jamet et al, 2006Jamet et al, , 2008a, together with detailed methodologies to optimize extraction (Feiz et al, 2006;Watson and Sumner, 2007;Jamet et al, 2008b). These have resulted in catalogs of proteins whose identity matches known functions associated with wall-related processes, such as polysaccharide modification, defense, and signaling, as well as many with unknown functions.…”

Section: Who Belongs To the Cell Wall Proteome?mentioning

confidence: 99%

Straying off the Highway: Trafficking of Secreted Plant Proteins and Complexity in the Plant Cell Wall Proteome

2010

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From simply skimming through the abstract lists of more or less any collection of both basic and applied plant-related journals, it is immediately apparent that the plant cell wall represents a nexus of many fields of research: growth and development, plant-pathogen interactions, abiotic stress, self-and interorganismal recognition, signaling systems, numerous primary and specialized metabolic processes, biomaterials and bioproducts, and many others. That said, and to deal with an issue of semantics, while the term cell wall can refer specifically to the structural matrix that surrounds all plant cells, for the purposes of this Update it is used more broadly, also to include the apoplast, or extracellular environment. Given its multifunctional nature then, it is not surprising that the apoplast houses a dynamic and complex proteome, and the compendium of cell wall proteins continues to grow as researchers from disparate disciplines discover new roles for extracellular proteins. In addition, however, as cell wall proteomics projects develop and the subcellular localizations of an ever-growing list of plant proteins are determined, a number of surprises have been thrown up, both in terms of the identity of secreted proteins and the trafficking pathways that they follow. The purpose of this Update is to give some examples of previously unsuspected aspects of plant cell wall protein trafficking that are challenging longheld assumptions, rather than to provide an exhaustive review, and to highlight some questions that can be categorized into the "who, how, where, and when" of the cell wall proteome.

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Cell wall proteins: a new insight through proteomics

Cited by 255 publications

References 76 publications

Lack of α-Xylosidase Activity in Arabidopsis Alters Xyloglucan Composition and Results in Growth Defects

Lack of α-Xylosidase Activity in Arabidopsis Alters Xyloglucan Composition and Results in Growth Defects

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

Straying off the Highway: Trafficking of Secreted Plant Proteins and Complexity in the Plant Cell Wall Proteome

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