Related Experiment Video
Updated: Jul 15, 2025
07:17
Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
17.4K
De novo designed Hsp70 activator dissolves intracellular condensates
Jason Z Zhang1,2,3, Nathan Greenwood1,2, Jason Hernandez4,5
1Department of Biochemistry, University of Washington, Seattle, Washington 98195, United States.
Biorxiv : the Preprint Server for Biology
|October 2, 2023
Summary
Researchers designed novel Hsp70-binding proteins to control protein quality control (PQC). These engineered proteins modulated Hsp70 activity and could dissolve cellular condensates, offering new ways to target PQC systems.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Protein quality control (PQC) relies on chaperones like Hsp70 and J-domain proteins (JDPs/Hsp40s).
- JDPs are believed to recruit Hsp70 to specific client proteins for PQC.
- The precise molecular mechanisms governing Hsp70-JDP interactions remain unclear.
Conclusions:
- The designed proteins provide insights into Hsp70 chaperone structure-function relationships.
- Engineered Hsp70 binders offer a modular approach to manipulate PQC.
- This strategy allows targeted delivery of PQC systems to specific cellular locations, including condensates.
