How Do J-Proteins Get Hsp70 to Do So Many Different Things?

@article{Craig2017HowDJ,
  title={How Do J-Proteins Get Hsp70 to Do So Many Different Things?},
  author={Elizabeth A Craig and J. Marszalek},
  journal={Trends in biochemical sciences},
  year={2017},
  volume={42 5},
  pages={355-368}
}
Hsp70 chaperone machineries have pivotal roles in an array of fundamental biological processes through their facilitation of protein folding, disaggregation, and remodeling. The obligate J-protein co-chaperones of Hsp70s drive much of this remarkable multifunctionality, with most Hsp70s having multiple J-protein partners. Recent data suggest that J-protein-driven versatility is substantially due to precise localization within the cell and the specificity of substrate protein binding. However… CONTINUE READING