ArticleJournal of the American Chemical Society2015
Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- A primordial synaptotagmin-independent function of complexin in regulated exocytosis.Nature communications · 2026Article
- Aggregation of Phosphates Enhances Enzyme Activity in Aqueous Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- MIRO1-mediated mitochondrial fusion is required for stomatal immunity in Arabidopsis.Nature plants · 2026Article
- A specific negatively charged sequence confers intramolecular regulation on Munc13-1 function in synaptic exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Uncovering the Mechanisms of Intracellular Membrane Trafficking by Reconstituted Membrane Systems.Membranes · 2025Review
- Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization.The Journal of cell biology · 2024Article
- SNARE chaperone Sly1 directly mediates close-range vesicle tethering.The Journal of cell biology · 2024Article
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
- Distinct Effects of Familial Parkinson's Disease-Associated Mutations on α-Synuclein Phase Separation and Amyloid Aggregation.Biomolecules · 2023Article
- Epigallocatechin gallate inhibits SNARE-dependent membrane fusion by blocking trans-SNARE assembly.FEBS open bio · 2022Article
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- Curcumin Interacts with α-Synuclein Condensates To Inhibit Amyloid Aggregation under Phase Separation.ACS omega · 2022Article
- Circularized fluorescent nanodiscs for probing protein-lipid interactions.Communications biology · 2022Article
- SNARE Zippering Is Suppressed by a Conformational Constraint that Is Removed by v-SNARE Splitting.Cell reports · 2021Article
- Programmable Extracellular Vesicles for Macromolecule Delivery and Genome Modifications.Developmental cell · 2020Article
- Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE.Cell reports · 2019Article
- Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartments.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin.Nature communications · 2019Article
- AAGAB Controls AP2 Adaptor Assembly in Clathrin-Mediated Endocytosis.Developmental cell · 2019Article
- Functional Reconstitution of Intracellular Vesicle Fusion Using Purified SNAREs and Sec1/Munc18 (SM) Proteins.Methods in molecular biology (Clifton, N.J.) · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Intracellular vesicle fusion is mediated by SNAREs and Sec1/Munc18 (SM) proteins. Despite intensive efforts, the SNARE-SM mediated vesicle fusion reaction has not been faithfully reconstituted in biochemical assays. Here, we present an unexpected discovery that macromolecular crowding is required for reconstituting the vesicle fusion reaction in vitro. Macromolecular crowding is known to profoundly influence the kinetic and thermodynamic behaviors of macromolecules, but its role in membrane transport processes such as vesicle fusion remains unexplored. We introduced macromolecular crowding agents into reconstituted fusion reactions to mimic the crowded cellular environment. In this crowded assay, SNAREs and SM proteins acted in concert to drive efficient membrane fusion. In uncrowded assays, by contrast, SM proteins failed to associate with the SNAREs and the fusion rate decreased more than 30-fold, close to undetectable levels. The activities of SM proteins were strictly specific to their cognate SNARE isoforms and sensitive to biologically relevant mutations, further supporting that the crowded fusion assay accurately recapitulates the vesicle fusion reaction. Using this crowded fusion assay, we also showed that the SNARE-SM mediated fusion reaction can be modulated by two additional factors: NSF and α-SNAP. These findings suggest that the vesicle fusion machinery likely has been evolutionarily selected to function optimally in the crowded milieu of the cell. Accordingly, macromolecular crowding should constitute an integral element of any reconstituted fusion assay.
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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.