Interaction between Cell Wall and Plasma Membrane via RGD Motif is Implicated in Plant Defense Responses

Kiba, Akinori; Sugimoto, Megumi; Toyoda, Kazuhiro; Ichinose, Yuki; Yamada, Tetsuji; Shiraishi, Takeshi

doi:10.1093/oxfordjournals.pcp.a029327

Cited by 52 publications

(29 citation statements)

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“…Hechtian strands are suggested to play significant roles in signal transduction and cell-cell communication events (Zandomeni and Schopfer, 1994;Reuzeau et al, 1997;Canut et al, 1998;Glass et al, 2000). In plants, application of Arg-GlyAsp peptides results in disruption of Hechtian strands accompanied by increased pathogen susceptibility (Mellersh and Heath, 2001) and loss in signaling between cell wall and plasma membrane (Kiba et al, 1998). Studies indicate that connections between the plasma membrane and cell wall can be mediated by a number of proteins, such as AGPs, wall-associated kinases, endo-1-4-b-D-glucanases, and cellulose synthases (Kjellbom et al, 1997;Kohorn, 2000Kohorn, , 2001.…”

Section: Discussionmentioning

confidence: 99%

Molecular Interactions of Arabinogalactan Proteins with Cortical Microtubules and F-Actin in Bright Yellow-2 Tobacco Cultured Cells

2006

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Arabinogalactan proteins (AGPs), a superfamily of plant hydroxyproline-rich glycoproteins, are present at cell surfaces. Although precise functions of AGPs remain elusive, they are widely implicated in plant growth and development. A well-characterized classical tomato (Lycopersicon esculentum) AGP containing a glycosylphosphatidylinositol plasma membrane anchor sequence was used here to elucidate functional roles of AGPs. Transgenic tobacco (Nicotiana tabacum) Bright Yellow-2 (BY-2) cells stably expressing green fluorescent protein (GFP)-LeAGP-1 were plasmolysed and used to localize LeAGP-1 on the plasma membrane and in Hechtian strands. Cytoskeleton disruptors and b-Yariv reagent (which binds and perturbs AGPs) were used to examine the role of LeAGP-1 as a candidate linker protein between the plasma membrane and cytoskeleton. This study used a two-pronged approach. First, BY-2 cells, either wild type or expressing GFP-microtubule (MT)-binding domain, were treated with b-Yariv reagent, and effects on MTs and F-actin were observed. Second, BY-2 cells expressing GFP-LeAGP-1 were treated with amiprophosmethyl and cytochalasin-D to disrupt MTs and F-actin, and effects on LeAGP-1 localization were observed. b-Yariv treatment resulted in terminal cell bulging, puncta formation, and depolymerization/disorganization of MTs, indicating a likely role for AGPs in cortical MT organization. b-Yariv treatment also resulted in the formation of thicker actin filaments, indicating a role for AGPs in actin polymerization. Similarly, amiprophosmethyl and cytochalasin-D treatments resulted in relocalization of LeAGP-1 on Hechtian strands and indicate roles for MTs and F-actin in AGP organization at the cell surface and in Hechtian strands. Collectively, these studies indicate that glycosylphosphatidylinositol-anchored AGPs function to link the plasma membrane to the cytoskeleton.

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Section: Discussionmentioning

confidence: 99%

Molecular Interactions of Arabinogalactan Proteins with Cortical Microtubules and F-Actin in Bright Yellow-2 Tobacco Cultured Cells

2006

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“…Thus, it is plausible that ToxA internalization relies on recognition of the RGD motif by a plant protein receptor. In fact, although plant genome sequencing has not revealed integrin homologs, immunologically related proteins exist (Faik et al, 1998;Kiba et al, 1998;Laboure et al, 1999;Laval et al, 1999;Nagpal and Quatrano, 1999;Swatzell et al, 1999;Sun et al, 2000;Baluska et al, 2003) and may provide candidates for mediating ToxA internalization. Deciphering the recognition mechanism of ToxA at the plasma membrane should help to clarify host susceptibility/resistance mechanisms and provide insight into the importance of the cell wall-plasma membrane-cytoskeleton continuum in host defense.…”

Section: Toxa Internalization Into Sensitive Wheat Cultivarsmentioning

confidence: 99%

Localization of Ptr ToxA Produced by Pyrenophora tritici-repentis Reveals Protein Import into Wheat Mesophyll Cells

2005

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The plant pathogenic fungus Pyrenophora tritici-repentis secretes host-selective toxins (HSTs) that function as pathogenicity factors. Unlike most HSTs that are products of enzymatic pathways, at least two toxins produced by P. tritici-repentis are proteins and, thus, products of single genes. Sensitivity to these toxins in the host is conferred by a single gene for each toxin. To study the site of action of Ptr ToxA (ToxA), toxin-sensitive and -insensitive wheat (Triticum aestivum) cultivars were treated with ToxA followed by proteinase K. ToxA was resistant to protease, but only in sensitive leaves, suggesting that ToxA is either protected from the protease by association with a receptor or internalized. Immunolocalization and green fluorescent protein tagged ToxA localization demonstrate that ToxA is internalized in sensitive wheat cultivars only. Once internalized, ToxA localizes to cytoplasmic compartments and to chloroplasts. Intracellular expression of ToxA by biolistic bombardment into both toxin-sensitive and -insensitive cells results in cell death, suggesting that the ToxA internal site of action is present in both cell types. However, because ToxA is internalized only in sensitive cultivars, toxin sensitivity, and therefore the ToxA sensitivity gene, are most likely related to protein import. The results of this study show that the ToxA protein is capable of crossing the plant plasma membrane from the apoplastic space to the interior of the plant cell in the absence of a pathogen.

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“…Such recognition is a general strategy that allows microorganisms to modulate infectivity and to regulate toxicity towards host cells [5]. Recent observations report that RGD peptides interfere with the activation of plant defence responses [13][14][15]. Thus, RGD recognition through plant proteins may occur and RGD-containing proteins from phytopathogenic microorganisms may act as pathogenicity factors.…”

Section: A B Cmentioning

confidence: 99%

“…Integrins are also chosen by pathogens as targets for binding, and the RGD motif is present in surface proteins of several pathogens that attach to mammalian cells [5]. In plants, synthetic peptides containing the RGD motif can disrupt the adhesion between plasma membrane and cell wall [6][7] and can interfere with physiological processes thereby affecting, e.g., development [8][9][10][11], mechano-perception [12] and the interaction with microorganisms [13][14][15]. In particular, expression of cell wall associated defence responses triggered by fungal pathogens is dependent on adhesion between the plasma membrane and the plant cell wall [15].…”

Section: Introductionmentioning

confidence: 99%

High affinity recognition of a Phytophthora protein by Arabidopsis via an RGD motif

Senchou

Weide

Carrasco

et al. 2004

Cellular and Molecular Life Sciences (CMLS)

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Interaction between Cell Wall and Plasma Membrane via RGD Motif is Implicated in Plant Defense Responses

Cited by 52 publications

References 0 publications

Molecular Interactions of Arabinogalactan Proteins with Cortical Microtubules and F-Actin in Bright Yellow-2 Tobacco Cultured Cells

Molecular Interactions of Arabinogalactan Proteins with Cortical Microtubules and F-Actin in Bright Yellow-2 Tobacco Cultured Cells

Localization of Ptr ToxA Produced by Pyrenophora tritici-repentis Reveals Protein Import into Wheat Mesophyll Cells

High affinity recognition of a Phytophthora protein by Arabidopsis via an RGD motif

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