The unfolded protein response in nutrient sensing and differentiation-Reference-Cited by-同舟云学术

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The unfolded protein response in nutrient sensing and differentiation

Published:2002-06 Issue:6 Volume:3 Page:411-421
ISSN:1471-0072
Container-title:Nature Reviews Molecular Cell Biology
language:en
Short-container-title:Nat Rev Mol Cell Biol

Author:

Kaufman Randal J.,Scheuner Donalyn,Schröder Martin,Shen Xiaohua,Lee Kyungho,Liu Chuan Yin,Arnold Stacey M.

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nrm829.pdf

Reference69 articles.

1. Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J. & Sambrook, J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462–464 (1988).

2. Dorner, A. J., Wasley, L. C. & Kaufman, R. J. Increased synthesis of secreted proteins induces expression of glucose regulated proteins in butyrate treated CHO cells. J. Biol. Chem. 264, 20602–20607 (1989).

3. Travers, K. J. et al. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101, 249–258 (2000).Microarray analysis of gene expression in response to accumulation of unfolded protein in yeast provided a complete picture of the functional groups of genes that are induced. In this analysis, it was determined that the upregulation of proteasome-mediated degradation is an important component of the UPR.

4. Kaufman, R. J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211–1233 (1999).

5. Prostko, C. R., Brostrom, M. A. & Brostrom, C. O. Reversible phosphorylation of eukaryotic initiation factor 2α in response to endoplasmic reticular signaling. Mol. Cell Biochem. 127–128, 255–265 (1993).

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