Measuring the effects of α1 -antitrypsin polymerisation on the structure and biophysical properties of the endoplasmic reticulum.


Type
Article
Change log
Authors
Chambers, Joseph E 
Dickens, Jennifer A 
Marciniak, Stefan J  ORCID logo  https://orcid.org/0000-0001-8472-7183
Abstract

An important function of the endoplasmic reticulum (ER) is to serve as a site of secretory protein folding. When the accumulation of misfolded proteins threatens to disturb luminal homoeostasis, the cell is said to experience ER stress. By contrast, the accumulation of well-folded proteins inside the ER leads to a distinct form of strain called ER overload. The serpins comprise a large family of proteins whose folding has been studied in great detail. Some mutant serpins misfold to cause ER stress, whereas others fold but then polymerise to cause ER overload. We discuss recent advances in the use of dynamic fluorescence imaging to study these phenomena. We also discuss a new technique that we recently published, rotor-based organelle viscosity imaging (ROVI), which promises to shed more light on the biophysical features of ER stress and ER overload.

Description
Keywords
ER overload, ER stress, Microviscosity, ROVI, α1-Antitrypsin, Animals, Biophysical Phenomena, Endoplasmic Reticulum, Humans, Inclusion Bodies, Polymerization, Viscosity, alpha 1-Antitrypsin
Journal Title
Biol Cell
Conference Name
Journal ISSN
0248-4900
1768-322X
Volume Title
110
Publisher
Wiley
Sponsorship
Medical Research Council (G1002610)
Medical Research Council (G0601840)
Alpha One Foundation (unknown)
Medical Research Council (MR/R009120/1)
Medical Research Council (G1000277)