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Updated: Aug 29, 2025
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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
Published on: July 17, 2019
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Sequestration of cellular native factors by biomolecular assemblies: Physiological or pathological?
1State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai 200031, PR China.
Biochimica Et Biophysica Acta. Molecular Cell Research
|September 10, 2022
Summary
Biomolecular assemblies, like liquid droplets and amyloid aggregates, sequester cellular factors. This process impacts cell function, homeostasis, and disease, offering new therapeutic targets.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- Biomolecules form dynamic supramolecular assemblies beyond native structures.
- These assemblies include liquid-like condensates and amyloid-like aggregates.
- They play crucial roles in cellular organization and function.
Purpose of the Study:
- To review recent advances in understanding biomolecular assembly sequestration.
- To discuss the consequences of this sequestration on cellular processes.
- To explore the link between assemblies, homeostasis, and disease pathology.
Main Methods:
- Literature review of recent scientific publications.
- Synthesis of findings on biomolecular assembly mechanisms.
- Analysis of the functional and pathological implications.
Main Results:
- Biomolecular assemblies sequester diverse native factors.
- Sequestration modulates cellular behaviors and homeostasis.
- Dysregulated sequestration is implicated in various disease pathologies.
Conclusions:
- Biomolecular assemblies are key regulators of cellular function.
- Understanding their sequestration mechanisms is vital for cell biology.
- Targeting these assemblies offers potential therapeutic strategies for diseases.
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