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Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms

Official URL:https://doi.org/10.1016/j.molcel.2010.10.001
PubMed:View item in PubMed
Creators Name:Buchberger, A. and Bukau, B. and Sommer, T.
Journal Title:Molecular Cell
Journal Abbreviation:Mol Cell
Volume:40
Number:2
Page Range:238-252
Date:22 October 2010
Keywords:Cytosol, Endoplasmic Reticulum, Eukaryotic Cells, Homeostasis, Biological Models, Molecular Chaperones, Protein Folding, Proteins, Animals
Abstract:In cells, both newly synthesized and pre-existing proteins are constantly endangered by misfolding and aggregation. The accumulation of damaged proteins can perturb cellular homeostasis and provoke aging, pathological states, and even cell death. To avert these dangers, cells have developed powerful quality control strategies that counteract protein damage in a compartment-specific way. Here, we compare the protein quality control systems of the eukaryotic cytosol and the endoplasmic reticulum, focusing on the principles of damage recognition, the triage decisions between chaperone-mediated refolding and proteolytic elimination of damaged proteins, the repair of misfolded and aggregated protein species, and the mechanisms by which perturbations of protein homeostasis are sensed to induce compartment-specific stress responses.
ISSN:1097-2765
Publisher:Cell Press (U.S.A.)
Item Type:Review

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