The unfolded protein response in nutrient sensing and differentiation

Kaufman, R.J.; Scheuner, D.; Schröder, M.; Shen, X.; Lee, K.; Liu, C.Y.; Arnold, S.M.

Abstract

Eukaryotic cells coordinate protein-folding reactions in the endoplasmic reticulum with gene expression in the nucleus and messenger RNA translation in the cytoplasm. As the rate of protein synthesis increases, protein folding can be compromised, so cells have evolved signal-transduction pathways that control transcription and translation -- the 'unfolded protein response'. Recent studies indicate that these pathways also coordinate rates of protein synthesis with nutrient and energy stores, and regulate cell differentiation to survive nutrient-limiting conditions or to produce large amounts of secreted products such as hormones, antibodies or growth factors.

Citation

Kaufman, R., Scheuner, D., Schröder, M., Shen, X., Lee, K., Liu, C., & Arnold, S. (2002). The unfolded protein response in nutrient sensing and differentiation. Nature Reviews Molecular Cell Biology, 3(6), 411-421. https://doi.org/10.1038/nrm829

• Journal Article Type: Article
• Publication Date: 2002-06
• Journal: Nature Reviews Molecular Cell Biology
• Print ISSN: 1471-0072
• Electronic ISSN: 1471-0080
• Publisher: Nature Research
• Peer Reviewed: Peer Reviewed
• Volume: 3
• Issue: 6
• Pages: 411-421
• DOI: https://doi.org/10.1038/nrm829
• Keywords: Unfolded protein response
• Public URL: https://durham-repository.worktribe.com/output/1597009