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 …
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 …
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) …
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 …
Neurotransmitter release—four years of SNARE complexes
PI Hanson, JE Heuser, R Jahn - Current opinion in neurobiology, 1997 - Elsevier
Exocytosis in neurons requires proteins known as SNAREs, membrane proteins that have
now been implicated in many intracellular fusion events. SNAREs assemble into stable …
now been implicated in many intracellular fusion events. SNAREs assemble into stable …
Binding of Munc18-1 to synaptobrevin and to the SNARE four-helix bundle
Y Xu, L Su, J Rizo - Biochemistry, 2010 - ACS Publications
Sec1/Munc18 (SM) proteins and soluble N-ethylmaleimide sensitive factor attachment
protein receptors (SNAREs) form part of the core intracellular membrane fusion machinery …
protein receptors (SNAREs) form part of the core intracellular membrane fusion machinery …
Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1: 1 syntaxin/SNAP-25 complex
K Weninger, ME Bowen, UB Choi, S Chu, AT Brunger - Structure, 2008 - cell.com
Syntaxin/SNAP-25 interactions precede assembly of the ternary SNARE complex that is
essential for neurotransmitter release. This binary complex has been difficult to characterize …
essential for neurotransmitter release. This binary complex has been difficult to characterize …
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 …
Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release
Neurotransmitter release depends critically on Munc18-1, Munc13, the Ca2+ sensor
synaptotagmin-1, and the soluble N-ethylmaleimide–sensitive factor (NSF) attachment …
synaptotagmin-1, and the soluble N-ethylmaleimide–sensitive factor (NSF) attachment …