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Chaperone-mediated assembly of the proteasome core particle - recent developments and structural insights
Helena M Schnell1, Richard M Walsh1,2,3, Shaun Rawson2,3
1Department of Pathology, Harvard Medical School and Brigham and Women's Hospital, 75 Francis Street, Boston, MA 02115, USA.
Journal of Cell Science
|April 22, 2022
Summary
The proteasome core particle (CP) assembly requires five specific chaperones in a precise, ordered pathway. This chaperone-mediated process is crucial for producing this essential cellular complex.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Cellular activities rely on large, multisubunit complexes.
- Complex assembly often requires dedicated chaperone proteins.
- The proteasome, essential for protein degradation, is one such complex.
Purpose of the Study:
- To review the biogenesis pathway of the proteasome core particle (CP).
- To highlight recent advances in understanding CP assembly, focusing on structural insights.
- To present CP biogenesis as a model for chaperone-mediated assembly.
Main Methods:
- Review of existing literature on proteasome biogenesis.
- Focus on structural data related to CP assembly.
- Analysis of the roles of specific chaperone proteins.
Main Results:
- Proteasome core particle (CP) biogenesis involves a highly ordered, multistep pathway.
- Five specific chaperones are essential for CP assembly.
- Recent structural insights have advanced the understanding of this complex process.
Conclusions:
- The pathway of CP biogenesis is a prime example of chaperone-mediated assembly.
- Understanding proteasome assembly provides a paradigm for constructing large molecular machines.
- Chaperones play a critical role in ensuring the proper formation of essential cellular complexes.
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