Abstract
Hsp70s are ubiquitous molecular chaperones that act in a myriad of cellular functions, affecting virtually all aspects in the life of proteins from synthesis to degradation. Hsp70 proteins act in the cell in cooperation with a large set of dedicated co-chaperones consisting of J-domain proteins and nucleotide exchange factors that regulate the Hsp70 chaperone cycle. Recent studies have made significant progress towards obtaining a better understanding of the mechanisms through which Hsp70s and their co-chaperones operate, providing insights into structural, kinetic, and functional features of the various members of this network. In this chapter we describe the emerging working principles of the Hsp70 machine and its co-chaperones, and highlight how mechanistic aspects of this network are tied to distinct protein folding functions.
| Original language | English |
|---|---|
| Title of host publication | HSF1 and Molecular Chaperones in Biology and Cancer |
| Publisher | Springer Nature |
| Pages | 3-20 |
| Number of pages | 18 |
| ISBN (Electronic) | 3030402045 |
| ISBN (Print) | 9783030402037 |
| DOIs | |
| Publication status | Published Online - 16 Apr 2020 |
Publication series
| Series | Advances in experimental medicine and biology |
|---|---|
| Volume | 1243 |
| ISSN | 0065-2598 |
Funding
R.R. is supported by the European Research Council starting grant (ERC-2018-STG 802001), the Azrieli Foundation, and a research grant from the Blythe Brenden-Mann New Scientist Fund.