Results 11 to 20 of about 72,246 (300)

Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly

open access: yesNature Communications, 2019
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
doaj   +2 more sources

Action of Complexin on SNARE Complex [PDF]

open access: yesJournal of Biological Chemistry, 2002
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
openaire   +2 more sources

Sequential analysis of trans-SNARE formation in intracellular membrane fusion. [PDF]

open access: yesPLoS Biology, 2012
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
doaj   +1 more source

HOPS recognizes each SNARE, assembling ternary trans-complexes for rapid fusion upon engagement with the 4th SNARE

open access: yeseLife, 2020
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
doaj   +1 more source

The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation

open access: yeseLife, 2020
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
doaj   +1 more source

The influence of cell membrane and SNAP25 linker loop on the dynamics and unzipping of SNARE complex. [PDF]

open access: yesPLoS ONE, 2017
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
doaj   +1 more source

Molecular Dynamics Simulations of the Proteins Regulating Synaptic Vesicle Fusion

open access: yesMembranes, 2023
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
doaj   +1 more source

Complex Lipid Requirements for SNARE- and SNARE Chaperone-dependent Membrane Fusion [PDF]

open access: yesJournal of Biological Chemistry, 2009
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
openaire   +2 more sources

Lysophosphatidylcholine inhibits membrane‐associated SNARE complex disassembly [PDF]

open access: yesJournal of Cellular and Molecular Medicine, 2012
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
openaire   +2 more sources

The role of the N-D1 linker of the N-ethylmaleimide-sensitive factor in the SNARE disassembly. [PDF]

open access: yesPLoS ONE, 2013
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
doaj   +1 more source

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