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
Original language | English |
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Pages (from-to) | 1463-1474 |
Journal | Journal of Proteomics |
Volume | 74 |
Issue number | 8 |
DOIs | |
Publication status | Published - 2011 |
Keywords
- protein-quality control
- capillary-electrophoresis
- endoplasmic-reticulum
- linked oligosaccharides
- mass-spectrometry
- oligosaccharyltransferase complex
- transmembrane topology
- glycosylated proteins
- monoclonal-antibody
- o-glycosylation