ArticlePloS one2015
Single particle fluorescence burst analysis of epsin induced membrane fission.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- GTP hydrolysis triggers membrane remodeling by AMPH-1.Science advances · 2025Article
- GTP-stimulated membrane fission by the N-BAR protein AMPH-1.Traffic (Copenhagen, Denmark) · 2023Article
- Development and application of multicolor burst analysis spectroscopy.Biophysical journal · 2021Article
- Mechanism of Cell Penetration by Permeabilization of Late Endosomes: Interplay between a Multivalent TAT Peptide and Bis(monoacylglycero)phosphate.Cell chemical biology · 2020Article
- Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019Review
- Efficient cell delivery mediated by lipid-specific endosomal escape of supercharged branched peptides.Traffic (Copenhagen, Denmark) · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
Vital cellular processes, from cell growth to synaptic transmission, rely on membrane-bounded carriers and vesicles to transport molecular cargo to and from specific intracellular compartments throughout the cell. Compartment-specific proteins are required for the final step, membrane fission, which releases the transport carrier from the intracellular compartment. The role of fission proteins, especially at intracellular locations and in non-neuronal cells, while informed by the dynamin-1 paradigm, remains to be resolved. In this study, we introduce a highly sensitive approach for the identification and analysis of membrane fission machinery, called burst analysis spectroscopy (BAS). BAS is a single particle, free-solution approach, well suited for quantitative measurements of membrane dynamics. Here, we use BAS to analyze membrane fission induced by the potent, fission-active ENTH domain of epsin. Using this method, we obtained temperature-dependent, time-resolved measurements of liposome size and concentration changes, even at sub-micromolar concentration of the epsin ENTH domain. We also uncovered, at 37°C, fission activity for the full-length epsin protein, supporting the argument that the membrane-fission activity observed with the ENTH domain represents a native function of the full-length epsin protein.
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Registered trials
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