Molecular chaperones and protein quality control: a thematic series
Coordinating Editors: Johannes Buchner and Norma Allewell
Cover figure: In the cell, different classes of molecular chaperones assist protein folding and prevent unwanted interactions between partially folded polypeptide chains. The different protein complexes interacting with partially folded proteins depict Hsp70, Hsp90 and small Hsps. In addition, polyphosphate chains, which were recently shown to have chaperone-like function, are shown bound to proteins. In some cases, two different molecular chaperones interact with the same polypeptide highlighting their network and team character. Structures [2KHO (Bertelsen et al., 2009 Proc.Natl.Acad.Sci.USA 106: 8471), 4YDZ (Fleckenstein et al., 2015 Mol.Cell 58: 1067), 5FWK (Verba et al., 2016 Science 352: 1542), 4V5F (Gao et al., 2009 Science 326: 694)] were created using the NGL Viewer (Rose et al., 2018 Bioinformatics 34: 3755) from the Protein Data Bank (www.rcsb.org; Berman et al., 2000 Nucleic Acids Res 28: 235) or adapted from the Molecule of the Month illustration by D.S. Goodsell. Artwork by Luciana Giono.
Molecular chaperones and protein quality control: an introduction to the JBC Reviews thematic series
Protein folding is a spontaneous process. However, under physiological conditions, proteins are inherently instable and the protein concentrations in the living cell 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.
Reviews in this Series: