The unfolded protein response in nutrient sensing and differentiation.
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.
Kaufman
Randal J
RJ
Department of Biological Chemistry, University of Michigan Medical Center, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109-0650, USA. kaufmanr@umich.edu
Scheuner
Donalyn
D
Schröder
Martin
M
Shen
Xiaohua
X
Lee
Kyungho
K
Liu
Chuan Yin
CY
Arnold
Stacey M
SM
D000818:Animals; D002454:Cell Differentiation; D002467:Cell Nucleus / Q000502:physiology*; D002468:Cell Physiological Phenomena; D014176:Protein Biosynthesis; D017510:Protein Folding; D011506:Proteins / Q000235:genetics* / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics; D014158:Transcription, Genetic
D011506:Proteins; D012333:RNA, Messenger