Plant Cell Wall Proteins

Cassab, Gladys I.

doi:10.1146/annurev.arplant.49.1.281

Cited by 501 publications

(438 citation statements)

References 142 publications

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“…Although quite a few Pro-rich proteins have been reported, the RePRP proteins described in this work are unique (Showalter, 1993;Cassab, 1998). First, the Pro content of rice RePRPs is around 40% for RePRP1 and 38% for RePRP2, significantly higher than that in the Pro-rich proteins so far reported.…”

Section: Reprps Are a Novel Class Of Highly Pro-rich Glycoproteins Exmentioning

confidence: 60%

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Abscisic Acid- and Stress-Induced Highly Proline-Rich Glycoproteins Regulate Root Growth in Rice

Tseng

Hong

et al. 2013

Plant Physiol.

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In the root of rice (Oryza sativa), abscisic acid (ABA) treatment, salinity, or water deficit stress induces the expression of a family of four genes, REPETITIVE PROLINE-RICH PROTEIN (RePRP). These genes encode two subclasses of novel proline-rich glycoproteins with highly repetitive PX 1 PX 2 motifs, RePRP1 and RePRP2. RePRP orthologs exist only in monocotyledonous plants, and their functions are virtually unknown. Rice RePRPs are heavily glycosylated with arabinose and glucose on multiple hydroxyproline residues. They are significantly different from arabinogalactan proteins that have glycan chains composed of arabinose and galactose. Transient and stable expressions of RePRP-green fluorescent protein reveal that a fraction of this protein is localized to the plasma membrane. In rice roots, ABA treatment increases RePRP expression preferentially in the elongation zone. Overexpression of RePRP in transgenic rice reduces root cell elongation in the absence of ABA, similar to the effect of ABA on wild-type roots. Conversely, simultaneous knockdown of the expression of RePRP1 and RePRP2 reduces the root sensitivity to ABA, indicating that RePRP proteins play an essential role in ABA/stress regulation of root growth and development. Moreover, rice RePRPs specifically interact with a polysaccharide, arabinogalactan, in a dosage-dependent manner. It is suggested that RePRP1 and RePRP2 are functionally redundant suppressors of root cell expansion and probably act through interactions with cell wall components near the plasma membrane.

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Section: Reprps Are a Novel Class Of Highly Pro-rich Glycoproteins Exmentioning

confidence: 60%

“…Plant hydroxyproline-rich glycoproteins (HRGPs) are the major structural proteins in cell walls (Showalter, 1993;Nothnagel, 1997;Cassab, 1998). Common features in HRGPs include enrichment in certain amino acids, repetitive sequence domains, and highly diverse carbohydrate contents.…”

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confidence: 99%

Abscisic Acid- and Stress-Induced Highly Proline-Rich Glycoproteins Regulate Root Growth in Rice

Tseng

Hong

et al. 2013

Plant Physiol.

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“…Four genes encode structural cell wall proteins (one Pro-rich protein and three extensins), which may strengthen the cell wall (Carpita and Gibeaut, 1993;Cassab, 1998). It remains to be shown whether the changes in gene expression are the cause of the visible phenotypes of rol1-2 plants.…”

Section: Rol1-1 and Rol1-2 Display Different Phenotypesmentioning

confidence: 99%

“…LRR domains are involved in proteinprotein interactions and are found in many proteins playing a role in disease resistance, signaling pathways, or the regulation of extracellular enzymes (Forsthoefel et al, 2005, and references therein). The C-terminal moiety of LRX proteins is composed of ] n repeats characteristic of Hyp-rich glycoproteins, which can modify the properties of the cell wall and might also play a role in connecting the cell wall with the plasma membrane by anchoring target proteins (Knox, 1995;Cassab, 1998). LRX1 is specifically expressed in root hairs and localizes to the cell wall where it is insolubilized (Baumberger et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

TheArabidopsisRoot Hair Cell Wall Formation Mutantlrx1Is Suppressed by Mutations in theRHM1Gene Encoding a UDP-L-Rhamnose Synthase

et al. 2006

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Cell and cell wall growth are mutually dependent processes that must be tightly coordinated and controlled. LRR-extensin1 (LRX1) of Arabidopsis thaliana is a potential regulator of cell wall development, consisting of an N-terminal leucine-rich repeat domain and a C-terminal extensin-like domain typical for structural cell wall proteins. LRX1 is expressed in root hairs, and lrx1 mutant plants develop distorted root hairs that often swell, branch, or collapse. The aberrant cell wall structures found in lrx1 mutants point toward a function of LRX1 during the establishment of the extracellular matrix. To identify genes that are involved in an LRX1-dependent developmental pathway, a suppressor screen was performed on the lrx1 mutant, and two independent rol1 (for repressor of lrx1) alleles were isolated. ROL1 is allelic to Rhamnose Biosynthesis1, which codes for a protein involved in the biosynthesis of rhamnose, a major monosaccharide component of pectin. The rol1 mutations modify the pectic polysaccharide rhamnogalacturonan I and, for one allele, rhamnogalacturonan II. Furthermore, the rol1 mutations cause a change in the expression of a number of cell wall-related genes. Thus, the lrx1 mutant phenotype is likely to be suppressed by changes in pectic polysaccharides or other cell wall components.

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“…Much less is known of vesicle trafficking and its control during wounding and pathogen attack, although the effects on secretion in plants is nonetheless dramatic. Wounding commonly leads to local deposition of callose, complex carbohydrates and lignification (Labavitch, 1981 ;Barber & Mitchell, 1997 ;Yang et al, 1997 ;Cassab, 1998). In some coenocytic algae, including Nitella and Vaucheria, wounding is followed by rapid mobilization of the cytoplasm, extracellular matrix material and membrane to the disturbed site (Walker, 1955 ;Foissner, 1988 ;Foissner, 1990 ;Crooks et al, 1999 ;M.…”

Section: Coupling Secretion To Cytosolic-free Ca# + Concentrationmentioning

confidence: 99%

Tansley Review No. 108

1999

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Eukaryotic cells share a set of secretory pathways for the flux of membrane and protein material. In 1993, ideas about the functioning of three major proteins of the neurosecretory complex were consolidated in the SNARE hypothesis, which proposed that the interaction of these proteins provides both the specificity for vesicle targeting and the molecular machinery for fusion between vesicle and target membranes. Subsequetly, the organization, molecular mechanics and control of vesicle trafficking have become topics of intense research, and the hypothesis has evolved to accommodate new discoveries from the analysis of secretion in yeast and mammals. It is likely to be challenged again as more information comes to light about secretory processes in plants. New tools for measuring and manipulating vesicle traffic and secretion are now being used, drawing on in vivo fluorescence and capacitance recording as well as genetic engineering. These new technologies have already begun to yield details wholly unexpected from past studies. Here we focus on recent findings relating to the mechanisms of vesicle trafficking and the background to these developments, highlighting both current understanding of the molecular events of secretion and the gaps therein, as well as discussing emerging themes from work with plants.

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Plant Cell Wall Proteins

Cited by 501 publications

References 142 publications

Abscisic Acid- and Stress-Induced Highly Proline-Rich Glycoproteins Regulate Root Growth in Rice

Abscisic Acid- and Stress-Induced Highly Proline-Rich Glycoproteins Regulate Root Growth in Rice

TheArabidopsisRoot Hair Cell Wall Formation Mutantlrx1Is Suppressed by Mutations in theRHM1Gene Encoding a UDP-L-Rhamnose Synthase

Tansley Review No. 108

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