Journal
CELL CHEMICAL BIOLOGY
Volume 23, Issue 8, Pages 992-1001Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2016.04.014
Keywords
-
Categories
Funding
- NIH [NS059690, GM109896]
- BrightFocus Foundation
- Tau Consortium
Ask authors/readers for more resources
Heat shock protein 70 (Hsp70) is a chaperone that normally scans the proteome and initiates the turnover of some proteins (termed clients) by linking them to the degradation pathways. This activity is critical to normal protein homeostasis, yet it appears to fail in diseases associated with abnormal protein accumulation. It is not clear why Hsp70 promotes client degradation under some conditions, while sparing that protein under others. Here, we used a combination of chemical biology and genetic strategies to systematically perturb the affinity of Hsp70 for the model client, tau. This approach revealed that tight complexes between Hsp70 and tau were associated with enhanced turnover while transient interactions favored tau retention. These results suggest that client affinity is one important parameter governing Hsp70-mediated quality control.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available