Protein quality control—linking the unfolded protein response to disease

The unfolded protein response

Where does the UPR function? Between the endoplasmic reticulum (ER) and the nucleus of eukaryotic cells. All secreted proteins and proteins that reside in secretory compartments translocate as nascent peptide chains into the ER, where they may undergo folding, modification and assembly before assuming their functional conformations. The ER maintains a specialized oxidizing environment to aid ch...

The unfolded protein response.

The endoplasmic reticulum (ER) is a principal site for folding and maturation of transmembrane, secretory and ERresident proteins. Perturbations that alter ER homeostasis can lead to accumulation of unfolded proteins (UPs), which is a threat to all living cells. To cope with the stress, cells activate an intracellular signaling pathway – the unfolded protein response (UPR). The UPR is an integr...

Protein quality control--linking the unfolded protein response to disease. Conference on 'From Unfolded Proteins in the Endoplasmic Reticulum to Disease'.

EMBO reports (2009) 10, 1206–1210. doi:10.1038/embor.2009.224 Introduction the correct folding of proteins is essential for cellular homeo stasis and the prevention of disease. During times of stress or changes in demand for newly synthesized proteins, signalling pathways co operate with networks of protein-folding and protein-degradation factors to maintain the pools of non-native proteins wit...

SnapShot: The Unfolded Protein Response

Unpacking the Unfolded Protein Response

This year, the Albert Lasker Basic Medical Research Award will be shared by Peter Walter and Kazutoshi Mori for discoveries revealing the molecular mechanism of the unfolded protein response, an intracellular quality control system that detects harmful misfolded proteins in the endoplasmic reticulum and then signals the nucleus to carry out corrective measures.