4.4 Review

Engineering eukaryotic protein factories

Journal

BIOTECHNOLOGY LETTERS
Volume 30, Issue 2, Pages 187-196

Publisher

SPRINGER
DOI: 10.1007/s10529-007-9524-1

Keywords

endoplasmic reticulum associated protein degradation; heterologous protein production; molecular chaperone; protein folding; unfolded protein response

Funding

  1. Biotechnology and Biological Sciences Research Council [BB/D01588X/1, BB/E006035/1, BB/C513418/1] Funding Source: researchfish
  2. BBSRC [BB/E006035/1, BB/D01588X/1] Funding Source: UKRI
  3. Biotechnology and Biological Sciences Research Council [BB/C513418/1, BB/D01588X/1] Funding Source: Medline
  4. Wellcome Trust [079821] Funding Source: Medline

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The biopharmaceuticals market is currently outperforming the pharmaceuticals market and is now valued at US$ 48 billion with an average annual growth of 19%. Behind this success is a 100-fold increase in productivities of eukaryotic expression systems. However, the productivity per cell has remained unchanged for more than 10 years. The engineering of the ER-resident protein folding machinery is discussed together with an overview of signal transduction pathways activated by heterologous protein overexpression to increase cell specific productivities.

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