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- Peter Walter
- Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA.
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- David Ron
- University of Cambridge, Metabolic Research Laboratory and NIHR Cambridge Biomedical Research Centre, Addenbrooke’s Hospital, Cambridge CB2 0QQ, UK.
書誌事項
- 公開日
- 2011-11-25
- DOI
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- 10.1126/science.1209038
- 公開者
- American Association for the Advancement of Science (AAAS)
この論文をさがす
説明
<jats:p>The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled proteins advance from the ER to the cell surface. To ascertain fidelity in protein folding, cells regulate the protein-folding capacity in the ER according to need. The ER responds to the burden of unfolded proteins in its lumen (ER stress) by activating intracellular signal transduction pathways, collectively termed the unfolded protein response (UPR). Together, at least three mechanistically distinct branches of the UPR regulate the expression of numerous genes that maintain homeostasis in the ER or induce apoptosis if ER stress remains unmitigated. Recent advances shed light on mechanistic complexities and on the role of the UPR in numerous diseases.</jats:p>
収録刊行物
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- Science
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Science 334 (6059), 1081-1086, 2011-11-25
American Association for the Advancement of Science (AAAS)