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Membrane‐directed molecular assembly of the neuronal SNARE complex [PDF]
Journal of Cellular and Molecular Medicine, 2011 Since the discovery and implication of N-ethylmaleimide-sensitive factor (NSF)-attachment protein receptor (SNARE) proteins in membrane fusion almost two decades ago, there have been significant efforts to understand their involvement at the molecular ...
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SNARE Complex Regulation by Phosphorylation
Cell Biochemistry and Biophysics, 2006SNAREs (soluble N-ethylmaleimide-sensitive fusion factor attachment protein receptors) are ubiquitous proteins that direct vesicular trafficking and exocytosis. In neurons, SNAREs act to mediate release of neurotransmitters, which is a carefully regulated process. Calcium influx has long been shown to be the key trigger of release.
Deborah A, Snyder +2 more
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Tethering the assembly of SNARE complexes
Trends in Cell Biology, 2014The fusion of transport vesicles with their target membranes is fundamental for intracellular membrane trafficking and diverse physiological processes and is driven by the assembly of functional soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes.
Hong, WanJin, Lev, Sima
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Modulation of the SNARE core complex by dopamine
Canadian Journal of Physiology and Pharmacology, 2000Communication between nerve cells in the brain occurs primarily through specialized junctions called synapses. Recently, many details of synaptic transmission have emerged. The identities of specific proteins important for synaptic vesicle release have now been established.
H, Fisher, J E, Braun
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The t-SNARE Complex: A Close Up
Cellular and Molecular Neurobiology, 2010The SNARE proteins, syntaxin, SNAP-25, and synaptobrevin have long been known to provide the driving force for vesicle fusion in the process of regulated exocytosis. Of particular interest is the initial interaction between SNAP-25 and syntaxin to form the t-SNARE heterodimer, an acceptor for subsequent synaptobrevin engagement.
Alison R, Dun +2 more
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Nature Communications, 2013 Formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex provides mechanical thrust for membrane fusion, but its molecular mechanism is still unclear.
Duyoung Min +2 more
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Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2016 Synaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) couple their stepwise folding to fusion of synaptic vesicles with plasma membranes.
Aleksander A Rebane +2 more
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SNARE complexes prepare for membrane fusion
Trends in Neurosciences, 2005According to a popular theory, the three presynaptic SNARE proteins (syntaxin 1, synaptobrevin 2 and SNAP-25) drive neuroexocytosis by forming a complex that forces vesicle and plasma membranes together. However, individual reactions in this process have been difficult to resolve.
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SNARE proteins are not excessive for the formation of post-Golgi SNARE complexes in HeLa cells
Molecular and Cellular Biochemistry, 2012To evaluate the role of SNARE proteins in the constitutive exocytosis, we knocked down syntaxin 3, 4, 5, 6, 7, and VAMP3, 5, 7, 8 with their siRNAs, and determined the cell-to-medium ratio of CLuc, a secreted luciferase of Cypridina noctiluca. Although the protein level of SNAREs in HeLa cells was markedly reduced by the siRNA treatment, the cell ...
Miki, Okayama +5 more
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Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p
Nature Structural Biology, 1998The fusion of intracellular transport vesicles with their target membranes requires the assembly of SNARE proteins anchored in the apposed membranes. Here we use recombinant cytoplasmic domains of the yeast SNAREs involved in Golgi to plasma membrane trafficking to examine this assembly process in vitro.
K L, Nicholson +5 more
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