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Structure, Function, and Biosynthesis of Plant Cell Wall Proteins
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Structure, Function, and Biosynthesis of Plant Cell Wall Proteins

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Cell Biology".

Deadline for manuscript submissions: closed (31 March 2023) | Viewed by 4640

Special Issue Editor

Dr. Li Tan

E-Mail Website
Guest Editor
Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA
Interests: structure, function, and biosynthesis of plant cell wall AGPs; crosslinks within plant wall polymers, especially between AGPs, pectins, and hemicelluloses

Special Issue Information

Dear Colleagues,

Although glycoproteins only account for about 10% of plant cell wall dry weight, they play essential roles in many biological processes ranging from plant growth to development. Plant cell wall glycoproteins, mainly hydroxyproline-rich glycoproteins (HRGPs), include arabinoglactan-proteins, extensins, and proline-rich glycoproteins (PRPs) with different proline/hydroxyproline (Hyp)-containing motifs on the polypeptides and different patterns of glycosylations. From the heavily arabinogalactansylated AGPs to the moderately arabinosylated extensins and the least glycosylated PRPs, their attached carbohydrates and formed epitopes covalently or non-covalently interact with the surrounding wall polymers. Thus, proline–hydroxylation and subsequent Hyp-O-glycosylation determine the trafficking, localization, and function of the matured HRGPs. Although numerous works have been carried out to characterize the structure, function, and biosynthesis of these wall glycoproteins, it is far from enough for us to understand their in vivo roles and corresponding mechanisms in plant cell walls. This Special Issue of Plants will continue and highlight our current research and understanding on the structure, function, and biosynthesis of HRGPs.

Dr. Li Tan
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Plants is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • hydroxyproline-rich glycoproteins (HRGPs)
  • arabinogalactan proteins (AGPs)
  • extensins
  • proline-rich glycoproteins (PRPs)
  • structural analysis
  • function characterization
  • biosynthesis

Published Papers (2 papers)

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Research

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11 pages, 1510 KiB  
Article
Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures
by Li Tan, Jianfeng Xu, Michael Held, Derek T. A. Lamport and Marcia Kieliszewski
Plants 2023, 12(5), 1036; https://doi.org/10.3390/plants12051036 - 24 Feb 2023
Cited by 3 | Viewed by 1663
Abstract
Arabinogalactan-proteins (AGPs) are members of the hydroxyproline-rich glycoprotein (HRGP) superfamily. They are heavily glycosylated with arabinogalactans, which are usually composed of a β-1,3-linked galactan backbone with 6-O-linked galactosyl, oligo-1,6-galactosyl, or 1,6-galactan side chains that are further decorated with arabinosyl, glucuronosyl, rhamnosyl, [...] Read more.
Arabinogalactan-proteins (AGPs) are members of the hydroxyproline-rich glycoprotein (HRGP) superfamily. They are heavily glycosylated with arabinogalactans, which are usually composed of a β-1,3-linked galactan backbone with 6-O-linked galactosyl, oligo-1,6-galactosyl, or 1,6-galactan side chains that are further decorated with arabinosyl, glucuronosyl, rhamnosyl, and/or fucosyl residues. Here, our work with Hyp-O-polysaccharides isolated from (Ser-Hyp)32-EGFP (enhanced green fluorescent protein) fusion glycoproteins overexpressed in transgenic Arabidopsis suspension culture is consistent with the common structural features of AGPs isolated from tobacco. In addition, this work confirms the presence of β-1,6-linkage on the galactan backbone identified previously in AGP fusion glycoproteins expressed in tobacco suspension culture. Furthermore, the AGPs expressed in Arabidopsis suspension culture lack terminal-rhamnosyl residues and have a much lower level of glucuronosylation compared with those expressed in tobacco suspension culture. These differences not only suggest the presence of distinct glycosyl transferases for AGP glycosylation in the two systems, but also indicate the existence of minimum AG structures for type II AG functional features. Full article
(This article belongs to the Special Issue Structure, Function, and Biosynthesis of Plant Cell Wall Proteins)
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Review

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15 pages, 2473 KiB  
Review
N-glycoproteins in Plant Cell Walls: A Survey
by Hélène San Clemente and Elisabeth Jamet
Plants 2022, 11(23), 3204; https://doi.org/10.3390/plants11233204 - 23 Nov 2022
Cited by 2 | Viewed by 2197
Abstract
Cell walls are an extracellular compartment specific to plant cells, which are not found in animal cells. Their composition varies between cell types, plant species, and physiological states. They are composed of a great diversity of polymers, i.e., polysaccharides, proteins, and lignins. Cell [...] Read more.
Cell walls are an extracellular compartment specific to plant cells, which are not found in animal cells. Their composition varies between cell types, plant species, and physiological states. They are composed of a great diversity of polymers, i.e., polysaccharides, proteins, and lignins. Cell wall proteins (CWPs) are major players involved in the plasticity of cell walls which support cell growth and differentiation, as well as adaptation to environmental changes. In order to reach the extracellular space, CWPs are transported through the secretory pathway where they may undergo post-translational modifications, including N-glycosylations on the Asn residues in specific motifs (Asn-X-Ser/Thr-X, with X≠Pro). This review aims at providing a survey of the present knowledge related to cell wall N-glycoproteins with (i) an overview of the experimental workflows, (ii) a selection of relevant articles dedicated to N-glycoproteomics, (iii) a description of the diversity of N-glycans, and (iv) a focus on the importance of N-glycans for CWP structure and/or function. Full article
(This article belongs to the Special Issue Structure, Function, and Biosynthesis of Plant Cell Wall Proteins)
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