Blm10 Protein Promotes Proteasomal Substrate Turnover by an Active Gating Mechanism

 
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Dange, Thomas
Smith, David
Noy, Tahel
Rommel, Philipp C.
Jurzitza, Lukas
Cordero, Radames B.
Legendre, Anne
Finley, Daniel
Goldberg, Alfred L.
Schmidt, Marion
Published Version
https://doi.org/10.1074/jbc.M111.300178
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Dange, Thomas, David Smith, Tahel Noy, Philipp C. Rommel, Lukas Jurzitza, Radames J. B. Cordero, Anne Legendre, Daniel Finley, Alfred L. Goldberg, and Marion Schmidt. 2011. “Blm10 Protein Promotes Proteasomal Substrate Turnover by an Active Gating Mechanism.” Journal of Biological Chemistry 286 (50): 42830–39. https://doi.org/10.1074/jbc.m111.300178.
Abstract
Background: Association of the proteasome core with activators regulates proteasome activity. Results: Blm10 association increases proteasome activity toward peptides and the unstructured proteasome substrate tau-441. This process is mediated by the C terminus of Blm10. Conclusion: C-terminal docking-mediated proteasome activation by Blm10 facilitates the turnover of peptide and protein substrates.Significance: Blm10 contributes to the regulation of proteasome activity.
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