1. Biochemistry and Chemical Biology
Download icon

Chaperones: Aggregation in the spotlight

  1. Zihao Wang
  2. Miranda Collier
  3. Justin Benesch  Is a corresponding author
  1. Department of Chemistry, Oxford University, United Kingdom
  2. Department of Biology, Stanford University, United States
Insight
Cite this article as: eLife 2021;10:e73586 doi: 10.7554/eLife.73586
1 figure

Figures

Hypothesis for a coherent mechanism of sHsp chaperone function.

Chaperones known as sHsps (colourful dots) can bind to proteins destabilised under stress conditions (‘substrates’; grey dots). They either encourage other proteins to gather with them in large protective complexes known as co-aggregates (‘aggregase’ activity; red, left); or they keep the proteins they bind apart from each other (‘holdase’ activity; blue, right) to stop these substrates from transitioning into toxic aggregates such as amyloid fibrils (grey arrows). These apparently incompatible models of chaperones’ activity can be reconciled by considering that they both aim to stop destabilised proteins from coming together in specific ways that are harmful to the cell. Sometimes, this aim is achieved by forming reversible liquid condensates requiring both aspects of sHsp function: there, the chaperones help to sequester the proteins and prevent them from becoming amyloid fibrils.

Download links

A two-part list of links to download the article, or parts of the article, in various formats.

Downloads (link to download the article as PDF)

Download citations (links to download the citations from this article in formats compatible with various reference manager tools)

Open citations (links to open the citations from this article in various online reference manager services)