ArticleMolecular biology of the cell2011
Topological arrangement of the intracellular membrane fusion machinery.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Exocytic machineries differentially control mediator release from allergen-triggered RBL-2H3 cells.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023Article
- Functional Reconstitution of Intracellular Vesicle Fusion Using Purified SNAREs and Sec1/Munc18 (SM) Proteins.Methods in molecular biology (Clifton, N.J.) · 2019Article
- RABIF/MSS4 is a Rab-stabilizing holdase chaperone required for GLUT4 exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.Nature communications · 2015Article
- Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding.Journal of the American Chemical Society · 2015Article
- APOL1 Kidney Disease Risk Variants: An Evolving Landscape.Seminars in nephrology · 2015Review
- The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation.The Journal of biological chemistry · 2014Article
- Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Synip arrests soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent membrane fusion as a selective target membrane SNARE-binding inhibitor.The Journal of biological chemistry · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) form a four-helix coiled-coil bundle that juxtaposes two bilayers and drives a basal level of membrane fusion. The Sec1/Munc18 (SM) protein binds to its cognate SNARE bundle and accelerates the basal fusion reaction. The question of how the topological arrangement of the SNARE helices affects the reactivity of the fusion proteins remains unanswered. Here we address the problem for the first time in a reconstituted system containing both SNAREs and SM proteins. We find that to be fusogenic a SNARE topology must support both basal fusion and SM stimulation. Certain topological combinations of exocytic SNAREs result in basal fusion but cannot support SM stimulation, whereas other topologies support SM stimulation without inducing basal fusion. It is striking that of all the possible topological combinations of exocytic SNARE helices, only one induces efficient fusion. Our results suggest that the intracellular membrane fusion complex is designed to fuse bilayers according to one genetically programmed topology.
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