Abstract
Background: The CHIP E3 ligase regulates Hsp70 pro-degradation activities. Results: The P269A CHIP U-box mutation induces CHIP oligomerization and modulates nucleotide- and substrate-dependent interactions between the TPR domain and Hsp70 C terminus. Conclusion: The U-box domain plays a key role in CHIP recruitment to Hsp70-client complexes, possibly by controlling oligomerization. Significance: Hsp70-CHIP substrate triage is governed by complex allosteric interactions between multiple domains in both proteins.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 31069-31079 |
| Number of pages | 11 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 43 |
| DOIs | |
| State | Published - Oct 25 2013 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Matsumura, Y., Sakai, J., & Skach, W. R. (2013). Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase. Journal of Biological Chemistry, 288(43), 31069-31079. https://doi.org/10.1074/jbc.M113.479345