ArticleThe Journal of cell biology2025
Fluorescence lifetime sorting reveals tunable enzyme interactions within cytoplasmic condensates.
Article in The Journal of cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Phasor-Based Spatio-Spectral Segmentation for Hyperspectral Fluorescence Microscopy.Journal of biophotonics · 2026Article
- Emerging trends of fluorescence lifetime imaging microscopy (FLIM): advances, challenges, and prospects.Biophysics reports · 2026Article
- Automated FLIM-FRET Segmentation Within RNP Condensates.Bio-protocol · 2026Article
- A Universal Protein Ladder for Standardization of Diverse FRET Assays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Progress and Prospects in FRET for the Investigation of Protein-Protein Interactions.Biosensors · 2025Review
- Microscopy-based techniques for studying the material properties of biomolecular condensates in the cellular environment.Biophysical reviews · 2025Review
- The role of RNA in the nanoscale organization of α-synuclein phase separation.NAR molecular medicine · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Ribonucleoprotein (RNP) condensates partition RNA and protein into multiple liquid phases. The multiphasic feature of condensate-enriched components creates experimental challenges for distinguishing membraneless condensate functions from the surrounding dilute phase. We combined fluorescence lifetime imaging microscopy (FLIM) with phasor plot filtering and segmentation to resolve condensates from the dilute phase. Condensate-specific lifetimes were used to track protein-protein interactions by measuring FLIM-Förster resonance energy transfer (FRET). We used condensate FLIM-FRET to evaluate whether mRNA decapping complex subunits can form decapping-competent interactions within P-bodies. Condensate FLIM-FRET revealed the presence of core subunit interactions within P-bodies under basal conditions and the disruption of interactions between the decapping enzyme (Dcp2) and a critical cofactor (Dcp1A) during oxidative stress. Our results show a context-dependent plasticity of the P-body interaction network, which can be rewired within minutes in response to stimuli. Together, our FLIM-based approaches provide investigators with an automated and rigorous method to uncover and track essential protein-protein interaction dynamics within RNP condensates in live cells.
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Registered trials
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