Membrane-proximal tryptophans of synaptobrevin II stabilize priming of secretory vesicles (Q85392206)

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17 February 2020

title

Membrane-proximal tryptophans of synaptobrevin II stabilize priming of secretory vesicles (English)

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17 February 2020

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17 February 2020

Maria Borisovska

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17 February 2020

Yvonne N Schwarz

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17 February 2020

Madhurima Dhara

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17 February 2020

Antonio Yarzagaray

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17 February 2020

Sandra Hugo

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17 February 2020

Daniele Narzi

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17 February 2020

Shirley W I Siu

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17 February 2020

Ralf Mohrmann

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17 February 2020

Dieter Bruns

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publication date

1 November 2012

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17 February 2020

published in

Journal of Neuroscience

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volume

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issue

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page(s)

15983-15997

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describes a project that uses

17 February 2020

ImageJ

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11 June 2022

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inferred from PubMed Central ID database lookup

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Ca2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin- and phospholipid-binding domain of synaptobrevin

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Dissection of three Ca2+-dependent steps leading to secretion in chromaffin cells from mouse adrenal slices

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Vesicular restriction of synaptobrevin suggests a role for calcium in membrane fusion

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v-SNAREs control exocytosis of vesicles from priming to fusion

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Close membrane-membrane proximity induced by Ca(2+)-dependent multivalent binding of synaptotagmin-1 to phospholipids

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Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles

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Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion.

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Conformation of the synaptobrevin transmembrane domain

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Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion.

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SNAREs--engines for membrane fusion

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Molecular anatomy of a trafficking organelle

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The coupling between synaptic vesicles and Ca2+ channels determines fast neurotransmitter release

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Determinants of synaptobrevin regulation in membranes

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Energetics and dynamics of SNAREpin folding across lipid bilayers

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v-SNARE Actions during Ca2+-Triggered Exocytosis

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SNARE-catalyzed fusion events are regulated by Syntaxin1A-lipid interactions

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A role for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex dimerization during neurosecretion

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Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion

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Sphingosine facilitates SNARE complex assembly and activates synaptic vesicle exocytosis

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Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusion

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Evidence that electrostatic interactions between vesicle-associated membrane protein 2 and acidic phospholipids may modulate the fusion of transport vesicles with the plasma membrane

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Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation

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Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis

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V-ATPase Membrane Sector Associates with Synaptobrevin to Modulate Neurotransmitter Release

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SNARE force synchronizes synaptic vesicle fusion and controls the kinetics of quantal synaptic transmission

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Fast vesicle fusion in living cells requires at least three SNARE complexes

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Docking and fast fusion of synaptobrevin vesicles depends on the lipid compositions of the vesicle and the acceptor SNARE complex-containing target membrane

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Caught in the Act: Visualization of SNARE‐Mediated Fusion Events in Molecular Detail

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Docking of LDCVs is modulated by lower intracellular [Ca2+] than priming

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12 December 2020

Membrane fusion intermediates via directional and full assembly of the SNARE complex

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Identifiers

DOI

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17 February 2020

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17 February 2020

PubMed publication ID

23136435

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