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      On the Potential Function of Type II Arabinogalactan O-Glycosylation in Regulating the Fate of Plant Secretory Proteins

      review-article
      Frontiers in Plant Science
      Frontiers Media S.A.
      FLA4, secretion, traffic, golgi apparatus, protein quality control

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          Abstract

          In a plant-specific mode of protein glycosylation, various sugars and glycans are attached to hydroxyproline giving rise to a variety of diverse O-glycoproteins. The sub-family of arabinogalactan proteins is implicated in a multitude of biological functions, however, the mechanistic role of O-glycosylation on AGPs by type II arabinogalactans is largely elusive. Some models suggest roles of the O-glycans such as in ligand-receptor interactions and as localized calcium ion store. Structurally different but possibly analogous types of protein O-glycosylation exist in animal and yeast models and roles for O-glycans were suggested in determining the fate of O-glycoproteins by affecting intracellular sorting or proteolytic activation and degradation. At present, only few examples exist that describe how the fate of artificial and endogenous arabinogalactan proteins is affected by O-glycosylation with type II arabinogalactans. In addition to other roles, these glycans might act as a molecular determinant for cellular localization and protein lifetime of many endogenous proteins.

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          Most cited references107

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          An Arabidopsis cell wall proteoglycan consists of pectin and arabinoxylan covalently linked to an arabinogalactan protein.

          Plant cell walls are comprised largely of the polysaccharides cellulose, hemicellulose, and pectin, along with ∼10% protein and up to 40% lignin. These wall polymers interact covalently and noncovalently to form the functional cell wall. Characterized cross-links in the wall include covalent linkages between wall glycoprotein extensins between rhamnogalacturonan II monomer domains and between polysaccharides and lignin phenolic residues. Here, we show that two isoforms of a purified Arabidopsis thaliana arabinogalactan protein (AGP) encoded by hydroxyproline-rich glycoprotein family protein gene At3g45230 are covalently attached to wall matrix hemicellulosic and pectic polysaccharides, with rhamnogalacturonan I (RG I)/homogalacturonan linked to the rhamnosyl residue in the arabinogalactan (AG) of the AGP and with arabinoxylan attached to either a rhamnosyl residue in the RG I domain or directly to an arabinosyl residue in the AG glycan domain. The existence of this wall structure, named ARABINOXYLAN PECTIN ARABINOGALACTAN PROTEIN1 (APAP1), is contrary to prevailing cell wall models that depict separate protein, pectin, and hemicellulose polysaccharide networks. The modified sugar composition and increased extractability of pectin and xylan immunoreactive epitopes in apap1 mutant aerial biomass support a role for the APAP1 proteoglycan in plant wall architecture and function.
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            Arabinogalactan-proteins: key regulators at the cell surface?

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              Structure and function of plant cell wall proteins.

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                Author and article information

                Contributors
                Journal
                Front Plant Sci
                Front Plant Sci
                Front. Plant Sci.
                Frontiers in Plant Science
                Frontiers Media S.A.
                1664-462X
                10 September 2020
                2020
                : 11
                : 563735
                Affiliations
                [1] Department of Applied Genetics and Cell Biology, Institute of Plant Biotechnology and Cell biology, University of Natural Resources and Life Sciences Vienna , Vienna, Austria
                Author notes

                Edited by: Breeanna Urbanowicz, University of Georgia, United States

                Reviewed by: Elisabeth Jamet, Université Toulouse III Paul Sabatier, France; Debarati Basu, Louisiana State University, United States

                *Correspondence: Georg J. Seifert, georg.seifert@ 123456boku.ac.at

                This article was submitted to Plant Proteomics and Protein Structural Biology, a section of the journal Frontiers in Plant Science

                Article
                10.3389/fpls.2020.563735
                7511660
                7c64ba3f-3b2f-455a-bbe3-41f541941d3d
                Copyright © 2020 Seifert

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 19 May 2020
                : 24 August 2020
                Page count
                Figures: 2, Tables: 0, Equations: 0, References: 124, Pages: 11, Words: 6288
                Funding
                Funded by: Austrian Science Fund 10.13039/501100002428
                Categories
                Plant Science
                Review

                Plant science & Botany
                fla4,secretion,traffic,golgi apparatus,protein quality control
                Plant science & Botany
                fla4, secretion, traffic, golgi apparatus, protein quality control

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