The ubiquitylation machinery of the endoplasmic reticulum

Christian Hirsch, Robert Gauss, Sabine C. Horn, Oliver Neuber and Thomas Sommer
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Christian Hirsch: Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10
Robert Gauss: Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10
Sabine C. Horn: Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10
Oliver Neuber: Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10
Thomas Sommer: Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10

Nature, 2009, vol. 458, issue 7237, 453-460

Abstract: Abstract As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains newly synthesized polypeptides and supports their maturation. Only properly folded proteins are released to their designated destinations. Proteins that cannot mature are left to accumulate, impairing the function of the ER. To maintain homeostasis, the protein-quality-control system singles out aberrant polypeptides and delivers them to the cytosol, where they are destroyed by the proteasome. The importance of this pathway is evident from the growing list of pathologies associated with quality-control defects in the ER.

Date: 2009
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DOI: 10.1038/nature07962

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