Abstract
Background: ATPase subunits mediate 26 S proteasome assembly and function. Results: Defective ATP binding by some ATPase subunits inhibits proteasome assembly, and proteasomes harboring an ATP binding-defective subunit are impaired for proteolysis, substrate-stimulated gating, and ATPase activity. Conclusion: The proteasome requires normal ATP binding for assembly and function. Significance: Protein substrates promote their own degradation by inducing ATP-dependent proteasome functions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3334-3345 |
| Number of pages | 12 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 5 |
| DOIs | |
| State | Published - Feb 1 2013 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Kim, Y. C., Li, X., Thompson, D., & Demartino, G. N. (2013). ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome. Journal of Biological Chemistry, 288(5), 3334-3345. https://doi.org/10.1074/jbc.M112.424788