Endoplasmic KDEL sequence

Several molecular strategies have been successful in increasing foreign protein production in cultured plant cells. These include using promoters for inducible expression [10, 12, 29], optimizing codon usage [30] and adding the KDEL sequence to ensure protein retention in the endoplasmic reticulum [31]. Application of different... 

Proteins produced in plant cells can remain within the cell or are secreted into the apoplast via the bulk transport (secretory) pathway. In whole plants, because levels of protein accumulated intracellularly, e. g. using the KDEL sequence to ensure retention in the endoplasmic reticulum, are often higher than when the product is secreted [58], foreign proteins are generally not directed for secretion. However, as protein purification from plant biomass is potentially much more difficult and expensive than protein recovery from culture medium, protein secretion is considered an advantage in tissue culture systems. For economic harvesting from the medium, the protein should be stable once secreted and should accumulate to high levels in the extracellular environment. 

PDI contains a C-terminal tetrapeptide sequence known as the endoplasmic retention signal, KDEL. This anchor mediates the interaction between plasma membrane and membranes of the Golgi apparatus via a KDEL receptor. The PDI KDEL receptor complex is recycled back into the endoplasmic reticulum (Xiao et al., 1999). It is thought that a saturation of the retention mechanism results in the secretion of PDI which is deposited on the cell membrane and stabilized by electrostatic interactions (Terada et al, 1995). The secreted PDI is termed cell surface PDI (csPDI)... 

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