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Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy
Published on: August 3, 2021
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Noise buffering by biomolecular condensates in glucose sensing
Kobi Simpson-Lavy1, Martin Kupiec1
1The Shmunis School of Biomedicine and Cancer Research, Tel Aviv University, Ramat Aviv, 69978, Israel.
Current Opinion in Cell Biology
|January 3, 2021
Summary
Cellular noise buffering uses protein aggregation to stabilize states like the cell cycle. Std1 protein regulation involves liquid drop sequestration, influenced by chaperones, anti-aggregases, and phosphorylation.
Area of Science:
- Cellular biology
- Biochemistry
- Molecular regulation
Background:
- Cellular processes require noise buffering for stability, seen in cell cycle and metabolic switches.
- Protein aggregation and condensation are increasingly recognized as key regulatory mechanisms.
- Std1, an activator of Snf1/AMPK kinase, plays a role in cellular regulation.
Purpose of the Study:
- To investigate the regulation of Std1 protein by its sequestration into liquid drop foci.
- To explore how foci of metabolic signaling and enzymatic proteins are regulated.
- To understand the role of chaperones, anti-aggregases, and phosphorylation in this regulatory process.
Main Methods:
- Observational studies of protein aggregation and liquid drop formation.
- Biochemical assays to analyze protein interactions and modifications.
- Genetic manipulation to assess the function of regulatory factors.
Main Results:
- Std1 protein is regulated through sequestration into liquid drop foci.
- Foci formation is modulated by chaperones, anti-aggregases, and phosphorylation.
- This mechanism contributes to the buffering of cellular processes against noise.
Conclusions:
- Protein liquid drops serve as a regulatory mechanism for key cellular proteins like Std1.
- Chaperones, anti-aggregases, and phosphorylation are critical in controlling these condensates.
- This highlights a novel layer of noise buffering in cellular signaling pathways.

