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Updated: Mar 22, 2026

4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Subcellular modulation of protein VlsE stability and folding kinetics
Jonathan Tai1, Kapil Dave2, Vincent Hahn3
1Department of Biochemistry, University of Illinois, Urbana, IL, USA.
Abstract:
The interior of a cell interacts differently with proteins than a dilute buffer because of a wide variety of macromolecules, chaperones, and osmolytes that crowd and interact with polypeptide chains. We compare folding of fluorescent constructs of protein VlsE among three environments inside cells. The nucleus increases the stability of VlsE relative to the cytoplasm, but slows down folding kinetics. VlsE is also more stable in the endoplasmic reticulum, but unlike PGK, tends to aggregate there. Although fluorescent-tagged VlsE and PGK show opposite stability trends from in vitro to the cytoplasm, their trends from cytoplasm to nucleus are similar.
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