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Cracking the Sugar Code: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells

Journal

FRONTIERS IN PLANT SCIENCE
Volume 12, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fpls.2021.640919

Keywords

Arabidopsis; glycosyltransferases; plant protein glycosylation; glycan arrays; O-glycosylation; N-glycosylation; glycosyl hydrolases; glycan functions

Categories

Funding

  1. Austrian Science Fund (FWF) [P31920-B22, P32332-B]
  2. German Research Council (DFG) [PF850/1-1, PF850/7-1]
  3. Australia Research Council [CE1101007]
  4. ANPCyT [PICT2016-0132, PICT2017-0066]
  5. Fondo Nacional de Desarrollo Cientifico y Tecnologico [1200010]
  6. Instituto Milenio iBio - Iniciativa Cientifica Milenio, MINECON
  7. Austrian Science Fund (FWF) [P31920, P32332] Funding Source: Austrian Science Fund (FWF)
  8. Australian Research Council [CE1101007] Funding Source: Australian Research Council

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Glycosylation is a crucial modification process that can alter the biological function of proteins and lipids, affecting the development and physiology of an organism. While challenges remain in understanding plant glycosylation, high throughput approaches may help to address these gaps, revolutionizing the identification and characterization of unknown plant glycosyltransferases and hydrolases.
Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.

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