Role of the Extensin Superfamily in Primary Cell Wall Architecture

Lamport, Derek T. A.; Kieliszewski, Marcia J.; Chen, Yuning; Cannon, Maura C.

doi:10.1104/pp.110.169011

Cited by 216 publications

(210 citation statements)

References 128 publications

(159 reference statements)

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“…We did not adjust MAAB, as we wanted to more readily observe HRGP variation; whether our classification reflects functional differences is as yet untested. Given the role of Y motifs in intermolecular and intramolecular cross-linking (Held et al, 2004;Lamport et al, 2011), both the arrangement and composition of SP n /Y motifs are likely to impact function. Therefore, the identification and characterization of the diversity of EXT motifs could guide important functional studies.…”

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confidence: 99%

“…In the highly glycosylated AGPs, large type II arabino-3,6-galactan polysaccharides (degree of polymerization, 30-120) are added to clustered, non-contiguous Hyp residues such as the SO, AO, TO, and VO repeats ( Fig. 1; Kieliszewski and Lamport, 1994;Lamport et al, 2011). The extent of glycosylation of PRPs remains unclear, as it has not been studied extensively.…”

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“…Chlamydomonas reinhardtii, 30% [w/w]; Roberts, 1974;Voigt et al, 2009), yet they are generally a minor component of land plant (embryophyte) walls (approximately 10% [w/w] in primary walls but less in secondary walls). Despite their low abundance in land plants, selected HRGPs have been shown to play important functional roles in, but not limited to, cell expansion, root growth and development, xylem differentiation, somatic embryogenesis, initiation of female gametogenesis, self-incompatibility, signaling, salt tolerance, and pathogen responses, (for review, see Fincher et al, 1983;Kieliszewski and Lamport, 1994;Majewska-Sawka and Nothnagel, 2000;Seifert and Roberts, 2007;Ellis et al, 2010;Lamport et al, 2011;Draeger et al, 2015;Velasquez et al, 2015;Basu, 2016a, 2016b). Not surprisingly, HRGPs have both fascinated and challenged researchers for decades.…”

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Pipeline to Identify Hydroxyproline-Rich Glycoproteins

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Intrinsically disordered proteins (IDPs) are functional proteins that lack a well-defined three-dimensional structure. The study of IDPs is a rapidly growing area as the crucial biological functions of more of these proteins are uncovered. In plants, IDPs are implicated in plant stress responses, signaling, and regulatory processes. A superfamily of cell wall proteins, the hydroxyprolinerich glycoproteins (HRGPs), have characteristic features of IDPs. Their protein backbones are rich in the disordering amino acid proline, they contain repeated sequence motifs and extensive posttranslational modifications (glycosylation), and they have been implicated in many biological functions. HRGPs are evolutionarily ancient, having been isolated from the protein-rich walls of chlorophyte algae to the cellulose-rich walls of embryophytes. Examination of HRGPs in a range of plant species should provide valuable insights into how they have evolved. Commonly divided into the arabinogalactan proteins, extensins, and proline-rich proteins, in reality, a continuum of structures exists within this diverse and heterogenous superfamily. An inability to accurately classify HRGPs leads to inconsistent gene ontologies limiting the identification of HRGP classes in existing and emerging omics data sets. We present a novel and robust motif and amino acid bias (MAAB) bioinformatics pipeline to classify HRGPs into 23 descriptive subclasses. Validation of MAAB was achieved using available genomic resources and then applied to the 1000 Plants transcriptome project (www.onekp.com) data set. Significant improvement in the detection of HRGPs using multiple-kmer transcriptome assembly methodology was observed. The MAAB pipeline is readily adaptable and can be modified to optimize the recovery of IDPs from other organisms.

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“…Extensins are the best characterized of the plant HRGPs and these are commonly arabinosylated by the HPAT family of O-glycosyltransferases before being arabinogalactosylated (Velasquez et al, 2011;OgawaOhnishi et al, 2013). Extensins are cross-linked at Tyr residues by peroxidases and processed by proteases which insolubilize and lock the extensins into the cell wall structure (Helm et al, 2008;Lamport et al, 2011). Extensins were originally isolated from elongating coleoptiles over 50 years ago (Lamport, 1963) and proposed to be involved in cell wall extensibility, but this has never been functionally confirmed (Lamport et al, 2011).…”

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“…Plant cell walls typically consist of a network of cellulose, hemicellulose, pectin, and lignin, but also contain many structural proteins of unknown function such as Hyp-rich glycoproteins (HRGPs; Lamport et al, 2011). This group of proteins includes Pro-rich proteins (PRPs), arabinogalactan proteins (AGPs), and extensins.…”

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Formation of the Stomatal Outer Cuticular Ledge Requires a Guard Cell Wall Proline-Rich Protein

et al. 2017

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(K.S.); 0000-0002-6438-9188 (R.S.); 0000-0002-9703-0745 (A.J.F.); 0000-0001-9972-5156 (J.E.G.).Stomata are formed by a pair of guard cells which have thickened, elastic cell walls to withstand the large increases in turgor pressure that have to be generated to open the pore that they surround. We have characterized FOCL1, a guard cell-expressed, secreted protein with homology to Hyp-rich cell wall proteins. FOCL1-GFP localizes to the guard cell outer cuticular ledge and plants lacking FOCL1 produce stomata without a cuticular ledge. Instead the majority of stomatal pores are entirely covered over by a continuous fusion of the cuticle, and consequently plants have decreased levels of transpiration and display drought tolerance. The focl1 guard cells are larger and less able to reduce the aperture of their stomatal pore in response to closure signals suggesting that the flexibility of guard cell walls is impaired. FOCL1 is also expressed in lateral root initials where it aids lateral root emergence. We propose that FOCL1 acts in these highly specialized cells of the stomata and root to impart cell wall strength at high turgor and/or to facilitate interactions between the cell wall and the cuticle.

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Plant Cell Walls

Ivakov

Persson

2012

Encyclopedia of Life Sciences

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Based in part on the previous version of this eLS article 'Plant Cell Walls' (2001) by Stephen C Fry.The cell wall is the outer coat that provides a tough protective casing of the plant cell. Decades of research efforts have contributed to our current understanding of cell wall structure and function. The cell wall is composed primarily of three major classes of polysaccharide: cellulose, hemicellulose and pectin, as well as structural proteins, and phenolic and aliphatic polymers. In addition to structural roles, the cell wall has a multitude of important functions in plants. For example, cell wall expansion and its regulation is the basis of cell and plant growth, the cell wall gives plant cells their characteristic shapes, and it is strongly involved in defence responses against pathogens and herbivores. Furthermore, recent studies indicate some novel and remarkable roles for the cell wall in sensing processes during pattern formation in plant development. This article provides a general summary of the current understanding of cell wall structure and function.

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Role of the Extensin Superfamily in Primary Cell Wall Architecture

Cited by 216 publications

References 128 publications

Pipeline to Identify Hydroxyproline-Rich Glycoproteins

Pipeline to Identify Hydroxyproline-Rich Glycoproteins

Formation of the Stomatal Outer Cuticular Ledge Requires a Guard Cell Wall Proline-Rich Protein

Plant Cell Walls

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