Premium
Measuring the effects of α 1 ‐antitrypsin polymerisation on the structure and biophysical properties of the endoplasmic reticulum
Author(s) -
Chambers Joseph E.,
Dickens Jennifer A.,
Marciniak Stefan J.
Publication year - 2018
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/boc.201800023
Subject(s) - endoplasmic reticulum , unfolded protein response , biology , organelle , protein folding , microbiology and biotechnology , biophysics , secretory protein , biochemistry , secretion
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.