NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin
eLife, 2018 SNARE complex disassembly by the ATPase NSF is essential for neurotransmitter release and other membrane trafficking processes. We developed a single-molecule FRET assay to monitor repeated rounds of NSF-mediated disassembly and reassembly of individual ...
Ucheor B Choi +6 more
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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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Epileptic Phenotypes Associated With SNAREs and Related Synaptic Vesicle Exocytosis Machinery
Frontiers in Neurology, 2022 SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptor) are an heterogeneous family of proteins that, together with their key regulators, are implicated in synaptic vesicle exocytosis and synaptic transmission. SNAREs represent the
Elisa Cali +3 more
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Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana [PDF]
, 2013 The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex formation.
De Rycke, Riet +7 more
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Molecular Dynamics Simulations of SNARE Complex Unzipping [PDF]
Biophysical Journal, 2014 The SNARE proteins facilitate biological membrane fusion. The neuronal SNARE proteins, namely VAMP-2, also called synaptobrevin 2, SNAP-25, and syntaxin-1A together form a coiled-coil complex. The formation of this SNARE complex is vital for vesicle-plasma membrane fusion resulting in neurotransmitter exocytosis.
Satyan Sharma, Manfred Lindau
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Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion. [PDF]
PLoS Genetics, 2018 The autophagosomal SNARE Syntaxin17 (Syx17) forms a complex with Snap29 and Vamp7/8 to promote autophagosome-lysosome fusion via multiple interactions with the tethering complex HOPS.
Szabolcs Takáts +7 more
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γ-synuclein is a novel player in the control of body lipid metabolism [PDF]
, 2013 Peer reviewedPublisher ...
Buchman, Vladimir L +3 more
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The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth. [PDF]
, 2010 Previous studies have implicated DTNBP1 as a schizophrenia susceptibility gene and its encoded protein, dysbindin, as a potential regulator of synaptic vesicle physiology.
Chan, LN +9 more
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The SNAREs vti1a and vti1b have distinct localization and SNARE complex partners [PDF]
European Journal of Cell Biology, 2002 Two mammalian proteins, vtila and vtilb, are homologous to the yeast Q-SNARE Vtilp which is part of several SNARE complexes in different transport steps. In vitro experiments suggest distinct functions for vtila and vtilb. Here we compared the subcellular localization of endogenous vtila and vtilb by immunofluorescence and immuno-electron microscopy ...
Kreykenbohm, V +4 more
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The destructive effect of botulinum neurotoxins on the SNARE protein: SNAP-25 and synaptic membrane fusion [PDF]
PeerJ, 2015 Synaptic exocytosis requires the assembly of syntaxin 1A and SNAP-25 on the plasma membrane and synaptobrevin 2 (VAMP2) on the vesicular membrane to bridge the two opposite membranes.
Bin Lu
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