N-glycoproteomics in plants: perspectives and challenges

J Proteomics. 2011 Aug 12;74(8):1463-74. doi: 10.1016/j.jprot.2011.05.007. Epub 2011 May 12.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Carbohydrate Sequence
  • Electrophoresis, Polyacrylamide Gel
  • Endoplasmic Reticulum / metabolism
  • Glycomics / methods*
  • Glycopeptides / metabolism
  • Glycoproteins / metabolism
  • Glycosylation
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / metabolism
  • Plant Proteins / metabolism*
  • Plants / metabolism*
  • Polysaccharides / metabolism
  • Proteomics / methods*

Substances

  • Glycopeptides
  • Glycoproteins
  • Plant Proteins
  • Polysaccharides
  • Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase