Probing the Formation and Liquid-to-Solid Transition of FUS Condensates via the Lifetimes of Fluorescent Proteins

Liquid-liquid phase separation (LLPS) of biomolecules is a fundamental cellular process that is essential for maintaining homeostasis and facilitating biochemical activities. On the other hand, aberrant phase separation alters condensate fluidity and causes a transition from liquid-like condensates to solid-like condensates, which may lead to the formation of the pathological aggregations often observed in neurodegenerative diseases. Condensate fluidity is usually assessed by the fluorescence recovery after photobleaching. Here, we reveal that the fluorescence lifetimes of several fluorescent proteins are sensitive to LLPS and the liquid-to-solid transition. Furthermore, we identify several key residues that regulate the sensitivity of fluorescence lifetimes toward phase separation. Thus, we apply fluorescence lifetime imaging microscopy (FLIM) to visualize LLPS and the liquid-to-solid transition in living cells, demonstrating that FLIM is a nondestructive method for tracking changes in condensate fluidity in real time.

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Publication Details

Journal
The Journal of Physical Chemistry Letters
Published
2025-03-31
DOI
https://doi.org/10.1021/acs.jpclett.5c00262
Citations
1
Primary Topic
RNA Research and Splicing
Type
article
Field-Weighted Citation Impact
0.81

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article

Probing the Formation and Liquid-to-Solid Transition of FUS Condensates via the Lifetimes of Fluorescent Proteins

Jinyao Ji, Kui Xu, Chunlai Chen, Wenjuan Wang
1 citations
The Journal of Physical Chemistry Letters
RNA Research and Splicing
0.81
article

Probing the Formation and Liquid-to-Solid Transition of FUS Condensates via the Lifetimes of Fluorescent Proteins

Jinyao Ji, Kui Xu, Chunlai Chen, Wenjuan Wang
article en
1 citations

Abstract

Liquid-liquid phase separation (LLPS) of biomolecules is a fundamental cellular process that is essential for maintaining homeostasis and facilitating biochemical activities. On the other hand, aberrant phase separation alters condensate fluidity and causes a transition from liquid-like condensates to solid-like condensates, which may lead to the formation of the pathological aggregations often observed in neurodegenerative diseases. Condensate fluidity is usually assessed by the fluorescence recovery after photobleaching. Here, we reveal that the fluorescence lifetimes of several fluorescent proteins are sensitive to LLPS and the liquid-to-solid transition. Furthermore, we identify several key residues that regulate the sensitivity of fluorescence lifetimes toward phase separation. Thus, we apply fluorescence lifetime imaging microscopy (FLIM) to visualize LLPS and the liquid-to-solid transition in living cells, demonstrating that FLIM is a nondestructive method for tracking changes in condensate fluidity in real time.

The Journal of Physical Chemistry LettersVol. 16(14)
Protein Technologies (United Kingdom) (GB), Center for Life Sciences (CN), State Key Laboratory of Membrane Biology, Tsinghua University (CN)
National Natural Science Foundation of China, National Key Research and Development Program of China
Openalex Percentile: Top 30%
RNA Research and Splicing
0.81
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Probing the Formation and Liquid-to-Solid Transition of FUS Condensates via the Lifetimes of Fluorescent Proteins — Jinyao Ji, Kui Xu, et al. · The Journal of Physical Chemistry Letters (2025) | TGRS Research Map | TGRS