Membrane Binding of α-Synuclein Stimulates Expansion of SNARE-Dependent Fusion Pore [PDF]
Frontiers in Cell and Developmental Biology, 2021 SNARE-dependent membrane fusion is essential for neurotransmitter release at the synapse. Recently, α-synuclein has emerged as an important regulator for membrane fusion. Misfolded α-synuclein oligomers are potent fusion inhibitors. However, the function
Ryan Khounlo +6 more
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Human LAMP1 accelerates Lassa virus fusion and potently promotes fusion pore dilation upon forcing viral fusion with non-endosomal membrane. [PDF]
PLoS Pathogens, 2022 Lassa virus (LASV) cell entry is mediated by the interaction of the virus glycoprotein complex (GPC) with alpha-dystroglycan at the cell surface followed by binding to LAMP1 in late endosomes. However, LAMP1 is not absolutely required for LASV fusion, as
You Zhang +2 more
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Fusion pore regulation by cAMP/Epac2 controls cargo release during insulin exocytosis [PDF]
eLife, 2019 Regulated exocytosis establishes a narrow fusion pore as initial aqueous connection to the extracellular space, through which small transmitter molecules such as ATP can exit.
Alenka Guček +6 more
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Local PI(4,5)P2 signaling inhibits fusion pore expansion during exocytosis
Cell Reports, 2023 Summary: Phosphatidylinositol(4,5)bisphosphate (PI(4,5)P2) is an important signaling phospholipid that is required for regulated exocytosis and some forms of endocytosis.
Muhmmad Omar-Hmeadi +2 more
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Myomerger promotes fusion pore by elastic coupling between proximal membrane leaflets and hemifusion diaphragm [PDF]
Nature Communications, 2021 Myomerger mediates the transition from the early hemifusion stage to complete fusion during the formation of multinucleated muscle cells. Here, authors use theoretical modeling and cell fusion experiments to show that Myomerger promotes a fusion pore by ...
Gonen Golani +8 more
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High transmembrane voltage raised by close contact initiates fusion pore [PDF]
Frontiers in Molecular Neuroscience, 2016 Membrane fusion lies at the heart of neuronal communication but the detailed mechanism of a critical step, fusion pore initiation, remains poorly understood.
Bing Bu +3 more
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Nascent fusion pore opening monitored at single-SNAREpin resolution. [PDF]
Proc Natl Acad Sci U S A, 2021 Significance Using our recently designed microfluidic setup, we investigated the early stage of SNAREpin-induced fusion. We discovered the existence of subsecond transient fusion pores with a well-defined subnanometer size that occur when one or two ...
Heo P +4 more
europepmc +2 more sources
Optimal Detection of Fusion Pore Dynamics Using Polarized Total Internal Reflection Fluorescence Microscopy [PDF]
Frontiers in Molecular Biosciences, 2021 The fusion pore is the initial narrow connection that forms between fusing membranes. During vesicular release of hormones or neurotransmitters, the nanometer-sized fusion pore may open-close repeatedly (flicker) before resealing or dilating irreversibly,
Joerg Nikolaus +12 more
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Stabilization of the SNARE Core by Complexin-1 Facilitates Fusion Pore Expansion [PDF]
Frontiers in Molecular Biosciences, 2021 In the neuron, neurotransmitter release is an essential function that must be both consistent and tightly regulated. The continuity of neurotransmitter release is dependent in large part on vesicle recycling. However, the protein factors that dictate the
Josh Pierson, Yeon-Kyun Shin
doaj +2 more sources
Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact. [PDF]
Nat Commun, 2021 Synaptotagmin 1 is a vesicle-anchored membrane protein that functions as the Ca2+ sensor for synchronous neurotransmitter release. In this work, an arginine containing region in the second C2 domain of synaptotagmin 1 (C2B) is shown to control the ...
Nyenhuis SB +7 more
europepmc +2 more sources