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Updated: Feb 11, 2026

A Fluorescence Fluctuation Spectroscopy Assay of Protein-Protein Interactions at Cell-Cell Contacts
Published on: December 1, 2018
Modulation of Protein-Interaction States through the Cell Cycle
Lingyun Dai1, Tianyun Zhao1, Xavier Bisteau2
1School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.
This study reveals dynamic protein interactions throughout the cell cycle using proteome-wide cellular thermal shift assay (CETSA). It uncovers key protein complex modulations critical for cell cycle progression and establishes CETSA as a powerful tool.
Area of Science:
- Cell Biology
- Proteomics
- Biochemistry
Background:
- Cell cycle progression relies on intricate biochemical processes.
- Protein expression levels offer limited insight into cellular event regulation.
- Understanding dynamic protein interactions is crucial for cell cycle research.
Purpose of the Study:
- To investigate changes in protein interaction states across different cell cycle phases.
- To establish proteome-wide cellular thermal shift assay (CETSA) as a method for studying protein interactions in intact cells.
- To uncover novel molecular details of cell cycle regulation.
Main Methods:
- Proteome-wide implementation of the cellular thermal shift assay (CETSA).
- Analysis of protein interaction states during specific cell cycle phases.
- Global profiling of protein expression and interactions.
Main Results:
- Identified changes in interaction states for over 750 proteins during the cell cycle.
- Revealed modulation of numerous protein complexes in specific cell cycle phases (e.g., DNA replication, chromatin remodeling, transcription, translation, nuclear envelope disintegration).
- Observed minimal differences in interaction states between G1 and G2 phases, suggesting conserved biochemical processes.
Conclusions:
- Protein complex modulation is a key feature of cell cycle progression.
- Proteome-wide CETSA is a valuable strategy for studying dynamic protein interactions in vivo.
- The study provides novel molecular insights into cell cycle regulation and protein complex dynamics.
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