Review
Nature Reviews Molecular Cell Biology 4, 181-191 (March 2003) | doi:10.1038/nrm1052
Quality control in the endoplasmic reticulum
Lars Ellgaard1 & Ari Helenius1 About the authors
Abstract
The endoplasmic reticulum (ER) has a quality-control system for 'proof-reading' newly synthesized proteins, so that only native conformers reach their final destinations. Non-native conformers and incompletely assembled oligomers are retained, and, if misfolded persistently, they are degraded. As a large fraction of ER-synthesized proteins fail to fold and mature properly, ER quality control is important for the fidelity of cellular functions. Here, we discuss recent progress in understanding the conformation-specific sorting of proteins at the level of ER retention and export.
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Author affiliations
- Institute of Biochemistry, Swiss Federal Institute of Technology (ETH) Zürich, Hönggerberg, CH - 8093 Zürich, Switzerland.
Correspondence to: Ari Helenius1 Email: ari.helenius@bc.biol.ethz.ch
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