title: Trafficking of endoplasmic reticulum-retained recombinant proteins is unpredictable in Arabidopsis thaliana.
abstract: A wide variety of recombinant proteins has been produced in the dicot model plant, Arabidopsis thaliana. Many of these proteins are targeted for secretion by means of an N-terminal endoplasmic reticulum (ER) signal peptide. In addition, they can also be designed for ER retention by adding a C-terminal H/KDEL-tag. Despite extensive knowledge of the protein trafficking pathways, the final protein destination, especially of such H/KDEL-tagged recombinant proteins, is unpredictable. In this respect, glycoproteins are ideal study objects. Microscopy experiments reveal their deposition pattern and characterization of their N-glycans aids in elucidating the trafficking. Here, we combine microscopy and N-glycosylation data generated in Arabidopsis leaves and seeds, and highlight the lack of a decent understanding of heterologous protein trafficking.
authors.affiliation: Department of Plant Systems Biology, VIB, Plant-made Antibodies and Immunogens Gent, Belgium ; Department of Plant Biotechnology and Bioinformatics, Ghent University Gent, Belgium.
authors.forename: Thomas
authors.initials: T
authors.lastname: De Meyer
authors.affiliation: Department of Plant Systems Biology, VIB, Plant-made Antibodies and Immunogens Gent, Belgium ; Department of Plant Biotechnology and Bioinformatics, Ghent University Gent, Belgium.
authors.forename: Ann
authors.initials: A
authors.lastname: Depicker
keywords: ER-derived vesicle; KDEL; antibody production; dense vesicle; molecular farming; protein storage vacuole; seed-specific expression