Results 11 to 20 of about 3,191 (253)
Negative regulation of syntaxin4/SNAP-23/VAMP2-mediated membrane fusion by Munc18c in vitro. [PDF]
PLoS ONE, 2008 Translocation of the facilitative glucose transporter GLUT4 from an intracellular store to the plasma membrane is responsible for the increased rate of glucose transport into fat and muscle cells in response to insulin. This represents a specialised form
Fiona M Brandie +5 more
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Cell Reports, 2019 Summary: Exocytosis of synaptic vesicles and dense-core vesicles requires both the Munc13 and CAPS (Ca2+-dependent activator proteins for secretion) proteins.
Hao Zhou +5 more
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Three-dimensional structure of the complexin/snare complex [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2002 During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca(2+)-evoked neurotransmitter ...
Chen, Xiaocheng +6 more
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Molecular Biology of the Cell, 2013 The fusion of yeast vacuolar membranes depends on the disassembly of cis–soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complexes and the subsequent reassembly of new SNARE complexes in trans. The disassembly of cis-SNARE complexes by Sec17/Sec18p releases the soluble SNARE Vam7p from vacuolar membranes.
Zick, Michael, Wickner, William
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The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation
eLife, 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
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Conformational change of Syntaxin-3b in regulating SNARE complex assembly in the ribbon synapses
Scientific Reports, 2022 Neurotransmitter release of synaptic vesicles relies on the assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, consisting of syntaxin and SNAP-25 on the plasma membrane and synaptobrevin on the synaptic
Claire Gething +6 more
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The influence of cell membrane and SNAP25 linker loop on the dynamics and unzipping of SNARE complex. [PDF]
PLoS 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
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eLife, 2020 The Ca2+ sensor synaptotagmin-1 and the SNARE complex cooperate to trigger neurotransmitter release. Structural studies elucidated three distinct synaptotagmin-1-SNARE complex binding modes involving ‘polybasic’, ‘primary’ and ‘tripartite’ interfaces of ...
Rashmi Voleti +2 more
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The role of the N-D1 linker of the N-ethylmaleimide-sensitive factor in the SNARE disassembly. [PDF]
PLoS 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
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Molecular Dynamics Simulations of the Proteins Regulating Synaptic Vesicle Fusion
Membranes, 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
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