Effects of Yariv phenylglycoside on cell wall assembly in the lily pollen tube

Roy, Stéphane; Jauh, Guang‐Yuh; Hepler, Peter K.; Lord, Elizabeth M.

doi:10.1007/s004250050279

Cited by 137 publications

(120 citation statements)

References 24 publications

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“…S5). AGPs play important roles in cell elongation, and b-Yariv inhibited the extension of tip-growing lily (Lilium longiflorum) pollen tubes and extension of apical cells of P. patens (Roy et al, 1998;Lee et al, 2005). Similarly, our results indicated a concentration-dependent inhibitory effect of b-Yariv on fiber elongation, suggesting that AGPs function in fiber development.…”

Section: Discussionsupporting

confidence: 67%

“…In Arabidopsis, 40% of GPI-anchored proteins contain arabinogalactan glycomodules, suggesting that AGPs may fulfill roles in intercellular signaling (Borner et al, 2003). Moreover, distinct classes of AGPs are involved in the complex interactions among different cell types in suspension cultures and act in pollen tube tip elongation, cell expansion, and moss cell tip elongation (Roy et al, 1998;Shi et al, 2003;Lee et al, 2005). In our study, transgenic cotton plants that carry a constitutively expressed 35S-GhFLA1 transgene produced longer fibers than wild-type plants.…”

Section: Discussionsupporting

confidence: 49%

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A Fasciclin-Like Arabinogalactan Protein, GhFLA1, Is Involved in Fiber Initiation and Elongation of Cotton

et al. 2013

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Arabinogalactan proteins (AGPs) are involved in many aspects of plant development. In this study, biochemical and genetic approaches demonstrated that AGPs are abundant in developing fibers and may be involved in fiber initiation and elongation. To further investigate the role of AGPs during fiber development, a fasciclin-like arabinogalactan protein gene (GhFLA1) was identified in cotton (Gossypium hirsutum). Overexpression of GhFLA1 in cotton promoted fiber elongation, leading to an increase in fiber length. In contrast, suppression of GhFLA1 expression in cotton slowed down fiber initiation and elongation. As a result, the mature fibers of the transgenic plants were significantly shorter than those of the wild type. In addition, expression levels of GhFLAs and the genes related to primary cell wall biosynthesis were remarkably enhanced in the GhFLA1 overexpression transgenic fibers, whereas the transcripts of these genes were dramatically reduced in the fibers of GhFLA1 RNA interference plants. An immunostaining assay indicated that both AGP composition and primary cell wall composition were changed in the transgenic fibers. The levels of glucose, arabinose, and galactose were also altered in the primary cell wall of the transgenic fibers compared with those of the wild type. Together, our results suggested that GhFLA1 may function in fiber initiation and elongation by affecting AGP composition and the integrity of the primary cell wall matrix.

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Section: Discussionsupporting

confidence: 67%

Section: Discussionsupporting

confidence: 49%

A Fasciclin-Like Arabinogalactan Protein, GhFLA1, Is Involved in Fiber Initiation and Elongation of Cotton

et al. 2013

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“…Moreover, transgenic tobacco plants successfully engineered for downregulated TTS expression demonstrated reduced pollen tube growth in the style and reduced seed production compared with wild-type plants [26]. In another set of experiments, Yariv reagent was applied to lily pollen tubes and shown to inhibit their growth and to produce a bulbous morphology at the pollen tube tip [70,71]. Furthermore, the normal influx of calcium at the tip was inhibited by the addition of Yariv reagent.…”

Section: Reproductive Growth and Developmentmentioning

confidence: 99%

Arabinogalactan-proteins: structure, expression and function

Showalter

2001

CMLS, Cell. Mol. Life Sci.

523

480

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Abstract. Arabinogalactan-proteins (AGPs) are a family of extensively glycosylated hydroxyproline-rich glycoproteins that are thought to have important roles in various aspects of plant growth and development. After a brief introduction to AGPs highlighting the problems associated with defining and classifying this diverse family of glycoproteins, AGP structure is described in terms of the protein component (including data from molecular cloning), carbohydrate component, processing of AGPs (including recent data on glycosylphosphatidylinositol membrane anchors) and overall molecular shape. Next, the expression of AGPs is examined at several different levels, from the whole plant to the cellular levels, using a variety of experimental techniques and tools. Finally, AGP function is considered. Although the existing functional evidence is not incontrovertible, it does clearly droxyproline poor, lightly glycosylated and largely unreactive with Yariv reagent. It is worth remembering that it is human nature to group and classify things to facilitate their comprehension and discourse, whereas Mother Nature simply constructs biological entities, including AGPs, using material at hand with blatant, pedagogical disregard. Structure Protein moietyKnowledge of the protein moieties of AGPs has mostly come from purifying AGPs, deglycosylating them and analyzing their respective core proteins by amino acid analysis and, to a more limited extent, by sequence analysis ( fig. 2) [3 -10]. More recently, molecular cloning of several confirmed and putative AGP core proteins has CMLS, Cell. Mol. Life Sci. 58 (2001) 1399 -1417 1420-682X/01/101399-19 $ 1.50 + 0.20/0 © Birkhäuser Verlag, Basel, 2001 CMLS Cellular and Molecular Life Sciences point to roles for AGPs in vegetative, reproductive, and cellular growth and development as well as programmed cell death and social control. In addition and most likely inextricably linked to their functions, AGPs are presumably involved in molecular interactions and cellular signaling at the cell surface. Some likely scenarios are discussed in this context. AGPs also have functions of real or potential commercial value, most notably as emulsifiers in the food industry and as potential immunological regulators for human health. Several important questions remain to be answered with respect to AGPs. Clearly, elucidating the unequivocal functions of particular AGPs and relating these functions to their respective structures and modes of action remain as major challenges in the years ahead.

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“…The major family of ␤-1,3-glucanases described here are related to pollen-specific ␤-1,3-glucanases (Huecas et al, 2001), and callose, a ␤-1,3-glucan, is an important polysaccharide in pollen walls (Rhee and Somerville, 1998). Furthermore, AGPs have also been shown to function in pollen growth (Roy et al, 1998;Bosch et al, 2001).…”

Section: Perspectivementioning

confidence: 99%

Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis

et al. 2002

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Glycosylphosphatidylinositol (GPI) anchoring of proteins provides a potential mechanism for targeting to the plant plasma membrane and cell wall. However, relatively few such proteins have been identified. Here, we develop a procedure for database analysis to identify GPI-anchored proteins (GAP) based on their possession of common features. In a comprehensive search of the annotated Arabidopsis genome, we identified 167 novel putative GAP in addition to the 43 previously described candidates. Many of these 210 proteins show similarity to characterized cell surface proteins. The predicted GAP include homologs of ␤-1,3-glucanases (16), metallo-and aspartyl proteases (13), glycerophosphodiesterases (6), phytocyanins (25), multi-copper oxidases (2), extensins (6), plasma membrane receptors (19), and lipid-transfer-proteins (18). Classical arabinogalactan (AG) proteins (13), AG peptides (9), fasciclin-like proteins (20), COBRA and 10 homologs, and novel potential signaling peptides that we name GAPEPs (8) were also identified. A further 34 proteins of unknown function were predicted to be GPI anchored. A surprising finding was that over 40% of the proteins identified here have probable AG glycosylation modules, suggesting that AG glycosylation of cell surface proteins is widespread. This analysis shows that GPI anchoring is likely to be a major modification in plants that is used to target a specific subset of proteins to the cell surface for extracellular matrix remodeling and signaling.Conventional membrane proteins possess one or more transmembrane domains that traverse the hydrophobic lipid bilayer. A glycosylphosphatidylinositol (GPI) anchor is an alternative means of attaching a protein to the membrane (for review, see Udenfriend and Kodukula, 1995), and it is found in all eukaryotic organisms. The C terminus of a GPIanchored protein (GAP) is covalently attached via phosphoethanolamine and a conserved glycan to phosphatidylinositol or a ceramide (Kinoshita and Inoue, 2000). GAPs have many features that distinguish them from proteins with transmembrane domains. The anchor can be removed by the action of specific phospholipases (Griffith and Ryan, 1999), converting the protein into a water-soluble form. In many organisms, they are found specifically at the outer leaflet of the plasma membrane (PM). It is important that GPI anchoring can target proteins to the PM in a polarized or localized manner, for example to the apical membrane of polarized mammalian epithelial cells (Le Gall et al., 1995) or the axon of neurons (Brown et al., 2000). As part of this targeting mechanism, GAPs are thought to associate with lipid rafts (Muniz and Riezman, 2000;Ikonen, 2001), and there is evidence for rafting of GAPs in plants ( Peskan et al., 2000). Therefore, this class of proteins forms a potentially important group of molecules involved in plant cell surface generation and remodeling (Sherrier et al., 1999).GAPs have only relatively recently been discovered in plants. Arabinogalactan (AG) proteins (AGPs), cell surface proteo...

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Effects of Yariv phenylglycoside on cell wall assembly in the lily pollen tube

Cited by 137 publications

References 24 publications

A Fasciclin-Like Arabinogalactan Protein, GhFLA1, Is Involved in Fiber Initiation and Elongation of Cotton

A Fasciclin-Like Arabinogalactan Protein, GhFLA1, Is Involved in Fiber Initiation and Elongation of Cotton

Arabinogalactan-proteins: structure, expression and function

Prediction of Glycosylphosphatidylinositol-Anchored Proteins in Arabidopsis. A Genomic Analysis

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