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Updated: Jan 31, 2026

Studying the Protein Quality Control System of D. discoideum Using Temperature-controlled Live Cell Imaging
Published on: December 2, 2016
Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic series
1From the Department of Chemistry, Technical University of Munich, 85747 Garching, Germany johannes.buchner@tum.de.
Abstract:
Protein folding is a spontaneous process. However, under physiological conditions, proteins are inherently unstable, and the protein concentrations in living cells favor unspecific interactions between partially folded proteins. Thus, the cellular proteome requires the assistance of helper factors, the molecular chaperones, for quality control and the maintenance of protein homeostasis. This series of reviews delves into how these molecular machines work in the eukaryotic cell, how they convey resilience to life, how these functions have allowed expansion of the protein universe, and how we can target them for therapeutic purposes. Together, they present the progress made in recent years in our understanding of one of the most fundamental aspects of life.
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