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Approaches to imaging unfolded secretory protein stress in living cells

100%

Lajoie P., Fazio E. N., Snapp E. L.

Endoplasmic Reticulum Stress in Diseases

2014

vol. 1

issue 1

The endoplasmic reticulum (ER) is the point of entry of proteins into the secretory pathway. Nascent peptides interact with the ER quality control machinery that ensures correct folding of the nascent proteins. Failure to properly fold proteins can lead to loss of protein function and cytotoxic aggregation of misfolded proteins that can lead to cell death. To cope with increases in the ER unfolded secretory protein burden, cells have evolved the Unfolded Protein Response (UPR). The UPR is the primary signaling pathway that monitors the state of the ER folding environment. When the unfolded protein burden overwhelms the capacity of the ER quality control machinery, a state termed ER stress, sensor proteins detect accumulation of misfolded peptides and trigger the UPR transcriptional response. The UPR, which is conserved from yeast to mammals, consists of an ensemble of complex signaling pathways that aims at adapting the ER to the new misfolded protein load. To determine how different factors impact the ER folding environment, various tools and assays have been developed. In this review, we discuss recent advances in live cell imaging reporters and model systems that enable researchers to monitor changes in the unfolded secretory protein burden and activation of the UPR and its associated signaling pathways.

From recordings of disulfide isomerases in action to reversal of maladaptive endoplasmic reticulum stress responses: proceedings on the ER & Redox Club Meeting held in Venice, April 2015

100%

van Anken E.

Endoplasmic Reticulum Stress in Diseases

2015

vol. 2

issue 1

The endoplasmic reticulum (ER) interacts and cooperates with other organelles as a central hub in cellular homeostasis. In particular, the ER is the first station along the secretory pathway, where client proteins fold and assemble before they travel to their final destination elsewhere in the endomembrane system or outside the cell. Protein folding and disulfide bond formation go hand in hand in the ER, a task that is achieved with the help of ER-resident chaperones and other folding factors, including oxidoreductases that catalyze disulfide bond formation. Yet, when their combined effort is in vain, client proteins that fail to fold are disposed of through ER-associated degradation (ERAD). The ER folding and ERAD machineries can be boosted through the unfolded protein response (UPR) if required. Still, protein folding in the ER may consistently fail when proteins are mutated due to a genetic defect, which, ultimately, can lead to disease. Novel developments in all these fields of study and how new insights ultimately can be exploited for clinical or biotechnological purposes were highlighted in a rich variety of presentations at the ER & Redox Club Meeting that was held in Venice from 15 to 17 April 2015. As such, the meeting provided the participants an excellent opportunity to mingle and discuss key advancements and outstanding questions on ER function in health and disease.

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2 Endoplasmic Reticulum Stress in Diseases

1 2015

1 2014

1 Fazio E. N.

1 Lajoie P.

1 Snapp E. L.

1 van Anken E.

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Approaches to imaging unfolded secretory protein stress in living cells

From recordings of disulfide isomerases in action to reversal of maladaptive endoplasmic reticulum stress responses: proceedings on the ER & Redox Club Meeting held in Venice, April 2015