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SUMO pathway is required for ribosome biogenesis.
1BK21 FOUR KNU Creative BioResearch Group, School of Life Sciences, College of National Sciences, Kyungpook National University, Daegu 41566; Brain Science and Engineering Institute, Kyungpook National University, Daegu 41566, Korea.
BMB Reports
|October 4, 2022
Summary
Small ubiquitin-related modifier (SUMO)ylation is crucial for regulating ribosome biogenesis. This process controls protein production by affecting ribosomal RNA and protein assembly, impacting gene expression and cellular functions.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Ribosomes are essential cellular machinery for protein synthesis, comprising proteins and ribosomal RNA (rRNA).
- Ribosome biogenesis involves intricate steps: transcription, rRNA maturation, and ribosomal protein assembly.
- Post-translational modifications, including SUMOylation, play a critical role in regulating factors essential for ribosome production.
Approach:
- This review synthesizes current research on the role of SUMOylation in ribosome biogenesis.
- It examines how SUMOylation targets proteins involved in ribosomal protein and rRNA gene expression, processing, and assembly.
- The impact of SUMOylation on the function and localization of these target proteins is discussed.
Key Points:
- SUMOylation is a key post-translational modification regulating ribosome biogenesis.
- It affects multiple stages, including gene expression of ribosomal components and assembly processes.
- SUMOylation influences the function and cellular localization of proteins critical for ribosome production.
Conclusions:
- SUMOylation is a vital regulatory mechanism in ribosome biogenesis.
- Understanding SUMOylation's role provides insights into cellular protein production control.
- This review highlights recent advancements in comprehending SUMOylation-mediated regulation of ribosome assembly.
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