The synaptic vesicle release machinery
Extensive research has yielded crucial insights into the mechanism of neurotransmitter
release, and working models for the functions of key proteins involved in release. The …
release, and working models for the functions of key proteins involved in release. The …
Mechanism of neurotransmitter release coming into focus
J Rizo - Protein Science, 2018 - Wiley Online Library
Research for three decades and major recent advances have provided crucial insights into
how neurotransmitters are released by Ca2+‐triggered synaptic vesicle exocytosis, leading …
how neurotransmitters are released by Ca2+‐triggered synaptic vesicle exocytosis, leading …
Molecular mechanisms underlying neurotransmitter release
J Rizo - Annual Review of Biophysics, 2022 - annualreviews.org
Major recent advances and previous data have led to a plausible model of how key proteins
mediate neurotransmitter release. In this model, the soluble N-ethylmaleimide-sensitive …
mediate neurotransmitter release. In this model, the soluble N-ethylmaleimide-sensitive …
Synaptic vesicle fusion
J Rizo, C Rosenmund - Nature structural & molecular biology, 2008 - nature.com
The core of the neurotransmitter release machinery is formed by SNARE complexes, which
bring the vesicle and plasma membranes together and are key for fusion, and by Munc18-1 …
bring the vesicle and plasma membranes together and are key for fusion, and by Munc18-1 …
Molecular mechanisms of fast neurotransmitter release
AT Brunger, UB Choi, Y Lai, J Leitz… - Annual review of …, 2018 - annualreviews.org
This review summarizes current knowledge of synaptic proteins that are central to synaptic
vesicle fusion in presynaptic active zones, including SNAREs (s oluble N-ethylmaleimide …
vesicle fusion in presynaptic active zones, including SNAREs (s oluble N-ethylmaleimide …
Snares and Munc18 in synaptic vesicle fusion
J Rizo, TC Südhof - Nature Reviews Neuroscience, 2002 - nature.com
The release of neurotransmitters by Ca2+-triggered synaptic vesicle exocytosis is an
exquisitely regulated process that is fundamental for interneuronal communication. This …
exquisitely regulated process that is fundamental for interneuronal communication. This …
Protein–protein interactions in neurotransmitter release
S Mochida - Neuroscience research, 2000 - Elsevier
The arrival of a nerve impulse at a nerve terminal leads to the opening of voltage-gated
Ca2+ channels and a rapid influx of Ca2+. The increase in Ca2+ concentration at the active …
Ca2+ channels and a rapid influx of Ca2+. The increase in Ca2+ concentration at the active …
Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes
R Guan, H Dai, J Rizo - Biochemistry, 2008 - ACS Publications
The core of the membrane fusion machinery that governs neurotransmitter release includes
the SNARE proteins syntaxin-1, SNAP-25 and synaptobrevin, which form a tight “SNARE …
the SNARE proteins syntaxin-1, SNAP-25 and synaptobrevin, which form a tight “SNARE …
Dual modes of Munc18-1/SNARE interactions are coupled by functionally critical binding to syntaxin-1 N terminus
M Khvotchev, I Dulubova, J Sun, H Dai… - Journal of …, 2007 - Soc Neuroscience
The SM (Sec1/Munc18-like) protein Munc18-1 and the soluble N-ethylmaleimide-sensitive
factor attachment protein (SNAP) receptor (SNARE) proteins syntaxin-1, SNAP-25, and …
factor attachment protein (SNAP) receptor (SNARE) proteins syntaxin-1, SNAP-25, and …
[HTML][HTML] Is assembly of the SNARE complex enough to fuel membrane fusion?
K Wiederhold, D Fasshauer - Journal of Biological Chemistry, 2009 - ASBMB
The three key players in the exocytotic release of neurotransmitters from synaptic vesicles
are the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) …
are the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) …