ArticleNature communications2019
Cycles of protein condensation and discharge in nuclear organelles studied by fluorescence lifetime imaging.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
- Automated FLIM-FRET Segmentation Within RNP Condensates.Bio-protocol · 2026Article
- High Molecular Crowding in Repair Foci Surrounding DNA Breaks, Measured by Fluorescence Lifetime Imaging Microscopy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Practical guide to fluorescence lifetime imaging microscopy.Molecular biology of the cell · 2025Review
- Fluorescence lifetime sorting reveals tunable enzyme interactions within cytoplasmic condensates.The Journal of cell biology · 2025Article
- Intermolecular energy migration via homoFRET captures the modulation in the material property of phase-separated biomolecular condensates.Nature communications · 2024Article
- Article
- Increased intracellular crowding during hyperosmotic stress.Scientific reports · 2023Article
- Exportin-inspired artificial cell nuclear-exporting nanosystems.Nanoscale advances · 2022Article
- Effect of Temperature on Re-entrant Condensation of Globular Protein in Presence of Tri-valent Ions.Journal of fluorescence · 2022Article
- Fluorescence lifetime imaging for studying DNA compaction and gene activities.Light, science & applications · 2021Article
- Physical Principles Underlying the Complex Biology of Intracellular Phase Transitions.Annual review of biophysics · 2020Review
- Monitoring the endocytosis of bovine serum albumin based on the fluorescence lifetime of small squaraine dye in living cells.Biomedical optics express · 2020Article
- Probing and engineering liquid-phase organelles.Nature biotechnology · 2019Review
- Protein folding and assembly in confined environments: Implications for protein aggregation in hydrogels and tissues.Biotechnology advancesReview
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear organelles are viscous droplets, created by concentration-dependent condensation and liquid-liquid phase separation of soluble proteins. Nuclear organelles have been actively investigated for their role in cellular regulation and disease. However, these studies are highly challenging to perform in live cells, and therefore, their physico-chemical properties are still poorly understood. In this study, we describe a fluorescence lifetime imaging approach for real-time monitoring of protein condensation in nuclear organelles of live cultured cells. This approach unravels surprisingly large cyclic changes in concentration of proteins in major nuclear organelles including nucleoli, nuclear speckles, Cajal bodies, as well as in the clusters of heterochromatin. Remarkably, protein concentration changes are synchronous for different organelles of the same cells. We propose a molecular mechanism responsible for synchronous accumulations of proteins in the nuclear organelles. This mechanism can serve for general regulation of cellular metabolism and contribute to coordination of gene expression.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.