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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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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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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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Fusion Machinery: SNARE Protein Complex
2014SNARE proteins constitute the minimal machinery needed for membrane fusion. SNAREs operate by forming a complex, which pulls the lipid bilayers into close contact and provides the mechanical force needed for lipid bilayer fusion. At the chemical synapse, SNARE-complex formation between the vesicular SNARE VAMP2/synaptobrevin-2 and the target (plasma ...
Sørensen, Jakob Balslev, Milosevic, Ira
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Buforin-1 blocks neuronal SNARE-mediated membrane fusion by inhibiting SNARE complex assembly
Biochemical and Biophysical Research Communications, 2019Assembly of neuronal SNARE protein complexes is essential for fusion of synaptic vesicles with the presynaptic plasma membrane, which releases neurotransmitters into the synaptic cleft and mediates neurotransmission. However, despite the potential of pharmacological regulation of this process for the treatment of various neurological disorders, only a ...
Jung Gi, Lee +5 more
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Molecular Dynamics Simulations of the SNARE Complex
2018Molecular dynamics (MD) simulations enable in silico investigations of the dynamic behavior of proteins and protein complexes. Here, we describe MD simulations of the SNARE complex and its interactions with the neuronal protein complexin. Complexin is an effector of neuronal secretion that inhibits spontaneous fusion and is thought to clamp the fusion ...
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Folding intermediates of SNARE complex assembly.
Nature structural biology, 1999SNARE (soluble NSF attachment protein receptor) proteins assemble into a stable complex essential for vesicle-membrane fusion. To further understand SNARE function we have used solution nuclear magnetic resonance (NMR) spectroscopy to characterize three assembly states of a yeast SNARE complex: first, the 'closed' conformation of Sso1; second, the ...
K M, Fiebig +3 more
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