N-glycoproteomics in plants: Perspectives and challenges

In eukaryotes, proteins that are secreted into the ER are mostly modified by N-glycans on consensus NxS/T sites. The N-linked glycan subsequently undergoes varying degrees of processing by enzymes which are spatially distributed over the ER and the Golgi apparatus. The post-ER N-glycan processing to...

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Bibliographic Details
Published in:Journal of proteomics 2011-08, Vol.74 (8), p.1463-1474
Main Authors: Song, Wei, Henquet, Maurice G.L., Mentink, Remco A., van Dijk, Aalt Jan, Cordewener, Jan H.G., Bosch, Dirk, America, Antoine H.P., van der Krol, Alexander R.
Format: Article
Language:English
Subjects:
animals
capillary-electrophoresis
Cell specific proteomics
endoplasmic-reticulum
enzymes
eukaryotic cells
Glycopeptides
glycoproteins
Glycoproteomics
glycosylated proteins
Golgi apparatus
linked oligosaccharides
Mass spectrometry
monoclonal-antibody
N-glycans
N-glycosylation
o-glycosylation
oligosaccharyltransferase complex
plant development
polysaccharides
protein-quality control
transmembrane topology
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Summary:In eukaryotes, proteins that are secreted into the ER are mostly modified by N-glycans on consensus NxS/T sites. The N-linked glycan subsequently undergoes varying degrees of processing by enzymes which are spatially distributed over the ER and the Golgi apparatus. The post-ER N-glycan processing to complex glycans differs between animals and plants, with consequences for N-glycan and glycopeptide isolation and characterization of plant glycoproteins. Here we describe some recent developments in plant glycoproteomics and illustrate how general and plant specific technologies may be used to address different important biological questions. [Display omitted] ► N-glycan core modifications in plants limit release of n-glycans by PNGases. ► Function N-glycan modifications in plants less clear as some mutants show no phenotype. ► Viable glycosylation mutants in plants allow for cell specific glycoproteomics strategies. ► Peptide identification software needs improvement for efficient identification isolated single glycopeptides.
ISSN:1874-3919
DOI:10.1016/j.jprot.2011.05.007