Review

Nature Reviews Molecular Cell Biology 3, 411-421 (June 2002) | doi:10.1038/nrm829

The unfolded protein response in nutrient sensing and differentiation

Randal J. Kaufman1,2, Donalyn Scheuner2, Martin Schröder2, Xiaohua Shen1, Kyungho Lee2, Chuan Yin Liu1 & Stacey M. Arnold1  About the authors

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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.

Author affiliations

  1. Department of Biological Chemistry, University of Michigan Medical Center, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109-0650, USA.
  2. Howard Hughes Medical Institute, University of Michigan Medical Center, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109-0650, USA.

Correspondence to: Randal J. Kaufman1,2 Email: kaufmanr@umich.edu

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