ArticleLangmuir : the ACS journal of surfaces and colloids2016
Using ApoE Nanolipoprotein Particles To Analyze SNARE-Induced Fusion Pores.
Article in Langmuir : the ACS journal of surfaces and colloids, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024Review
- Isolation of recombinant apolipoprotein E4 N-terminal domain by foam fractionation.Protein expression and purification · 2023Article
- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- One-step construction of circularized nanodiscs using SpyCatcher-SpyTag.Nature communications · 2021Article
- The neuronal calcium sensor Synaptotagmin-1 and SNARE proteins cooperate to dilate fusion pores.eLife · 2021Article
- TRIM67 regulates exocytic mode and neuronal morphogenesis via SNAP47.Cell reports · 2021Article
- Optimal Detection of Fusion Pore Dynamics Using Polarized Total Internal Reflection Fluorescence Microscopy.Frontiers in molecular biosciences · 2021Article
- Hrd1 forms the retrotranslocation pore regulated by auto-ubiquitination and binding of misfolded proteins.Nature cell biology · 2020Article
- SNARE-Mediated Exocytosis in Neuronal Development.Frontiers in molecular neuroscience · 2020Review
- A Nanodisc-Cell Fusion Assay with Single-Pore Sensitivity and Sub-millisecond Time Resolution.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Toward a unified picture of the exocytotic fusion pore.FEBS letters · 2018Review
- Article
- Amperometry methods for monitoring vesicular quantal size and regulation of exocytosis release.Pflugers Archiv : European journal of physiology · 2018Review
- Article
- Lipids Activate SecA for High Affinity Binding to the SecYEG Complex.The Journal of biological chemistry · 2016Article
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Authors and funding
4 authors.
Funding
Abstract
Here we introduce ApoE-based nanolipoprotein particle (NLP)-a soluble, discoidal bilayer mimetic of ∼23 nm in diameter, as fusion partners to study the dynamics of fusion pores induced by SNARE proteins. Using in vitro lipid mixing and content release assays, we report that NLPs reconstituted with synaptic v-SNARE VAMP2 (vNLP) fuse with liposomes containing the cognate t-SNARE (Syntaxin1/SNAP25) partner, with the resulting fusion pore opening directly to the external buffer. Efflux of encapsulated fluorescent dextrans of different sizes show that unlike the smaller nanodiscs, these larger NLPs accommodate the expansion of the fusion pore to at least ∼9 nm, and dithionite quenching of fluorescent lipid introduced in vNLP confirms that the NLP fusion pores are short-lived and eventually reseal. The NLPs also have capacity to accommodate larger number of proteins and using vNLPs with defined number of VAMP2 protein, including physiologically relevant copy numbers, we find that 3-4 copies of VAMP2 (minimum 2 per face) are required to keep a nascent fusion pore open, and the SNARE proteins act cooperatively to dilate the nascent fusion pore.
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Registered trials
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