Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly
Synaptic exocytosis depends on formation of the SNARE complex but its assembly mechanism is still under debate. Here, the authors identify an interaction between Munc13-1 and synaptobrevin-2 that is critical for the transition of the Munc18-1/syntaxin-1 ...
Shen Wang +6 more
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Action of Complexin on SNARE Complex [PDF]
Calcium-dependent synaptic vesicle exocytosis requires three SNARE (soluble N-ethylmaleimide-sensitive-factor attachment protein receptor) proteins: synaptobrevin/vesicle-associated membrane protein in the vesicular membrane and syntaxin and SNAP-25 in the presynaptic membrane.
Kuang, Hu +3 more
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Sequential analysis of trans-SNARE formation in intracellular membrane fusion. [PDF]
SNARE complexes are required for membrane fusion in the endomembrane system. They contain coiled-coil bundles of four helices, three (Q(a), Q(b), and Q(c)) from target (t)-SNAREs and one (R) from the vesicular (v)-SNARE.
Kannan Alpadi +7 more
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Yeast vacuole fusion requires R-SNARE, Q-SNAREs, and HOPS. A HOPS SM-family subunit binds the R- and Qa-SNAREs. We now report that HOPS binds each of the four SNAREs.
Hongki Song +4 more
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The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation
Fusion of intracellular trafficking vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes. SNARE-mediated membrane fusion requires Sec1/Munc18-family (SM) proteins, SNARE chaperones that can function as templates to ...
Travis J Eisemann +5 more
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The influence of cell membrane and SNAP25 linker loop on the dynamics and unzipping of SNARE complex. [PDF]
The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex is composed of three neuronal proteins VAMP2, Syntaxin and SNAP25, which plays a core role during the process of membrane fusion.
Yi Shi, Yong Zhang, Jizhong Lou
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Molecular Dynamics Simulations of the Proteins Regulating Synaptic Vesicle Fusion
Neuronal transmitters are packaged in synaptic vesicles (SVs) and released by the fusion of SVs with the presynaptic membrane (PM). An inflow of Ca2+ into the nerve terminal triggers fusion, and the SV-associated protein Synaptotagmin 1 (Syt1) serves as ...
Maria Bykhovskaia
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Complex Lipid Requirements for SNARE- and SNARE Chaperone-dependent Membrane Fusion [PDF]
Membrane fusion without lysis has been reconstituted with purified yeast vacuolar SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors), the SNARE chaperones Sec17p/Sec18p and the multifunctional HOPS complex, which includes a subunit of the SNARE-interactive Sec1-Munc18 family, and vacuolar lipids: phosphatidylcholine (PC ...
Joji, Mima, William, Wickner
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Lysophosphatidylcholine inhibits membrane‐associated SNARE complex disassembly [PDF]
AbstractIn cells, N‐ethylmaleimide‐sensitive factor (NSF) attachment protein receptors called SNAREs are involved in membrane fusion. In neurons, for example, target membrane proteins SNAP‐25 and syntaxin called t‐SNAREs present at the pre‐synaptic membrane, and a synaptic vesicle‐associated membrane protein (VAMP) or v‐SNARE, is part of the conserved ...
Shin, Leah +5 more
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The role of the N-D1 linker of the N-ethylmaleimide-sensitive factor in the SNARE disassembly. [PDF]
N-ethylmaleimide-sensitive factor (NSF) is a member of the type II AAA+ (ATPase associated with various cellular activities) family. It plays a critical role in intracellular membrane trafficking by disassembling soluble NSF attachment protein receptor ...
Cui-Cui Liu, Shan Sun, Sen-Fang Sui
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