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Front Plant Sci. 2014 Sep 15;5:473. doi: 10.3389/fpls.2014.00473. eCollection 2014.

Trafficking of endoplasmic reticulum-retained recombinant proteins is unpredictable in Arabidopsis thaliana.

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Department of Plant Systems Biology, VIB, Plant-made Antibodies and Immunogens Gent, Belgium ; Department of Plant Biotechnology and Bioinformatics, Ghent University Gent, Belgium.


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.


ER-derived vesicle; KDEL; antibody production; dense vesicle; molecular farming; protein storage vacuole; seed-specific expression

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