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 …
The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices—guilty as charged?
J Rizo, TC Südhof - Annual review of cell and developmental …, 2012 - annualreviews.org
Neurotransmitter release is governed by proteins that have homo-logs in most types of
intracellular membrane fusion, including the Sec1/Munc18 protein Munc18-1 and the …
intracellular membrane fusion, including the Sec1/Munc18 protein Munc18-1 and the …
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 …
Membrane fusion intermediates via directional and full assembly of the SNARE complex
JM Hernandez, A Stein, E Behrmann, D Riedel… - Science, 2012 - science.org
Cellular membrane fusion is thought to proceed through intermediates including docking of
apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and …
apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and …
Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion
The molecular underpinnings of synaptic vesicle fusion for fast neurotransmitter release are
still unclear. Here, we used a single vesicle–vesicle system with reconstituted SNARE and …
still unclear. Here, we used a single vesicle–vesicle system with reconstituted SNARE and …
A cascade of multiple proteins and lipids catalyzes membrane fusion
W Wickner, J Rizo - Molecular biology of the cell, 2017 - Am Soc Cell Biol
Recent studies suggest revisions to the SNARE paradigm of membrane fusion. Membrane
tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE …
tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE …
Autoinhibition of Munc18-1 modulates synaptobrevin binding and helps to enable Munc13-dependent regulation of membrane fusion
Munc18-1 orchestrates SNARE complex assembly together with Munc13-1 to mediate
neurotransmitter release. Munc18-1 binds to synaptobrevin, but the relevance of this …
neurotransmitter release. Munc18-1 binds to synaptobrevin, but the relevance of this …
Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins
H Yu, SS Rathore, JA Lopez… - Proceedings of the …, 2013 - National Acad Sciences
Sec1/Munc18 (SM) family proteins are essential for every vesicle fusion pathway. The best-
characterized SM protein is the synaptic factor Munc18-1, but it remains unclear whether its …
characterized SM protein is the synaptic factor Munc18-1, but it remains unclear whether its …
The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis
The fusion of neurotransmitter-filled synaptic vesicles with the plasma membrane requires
two classes of molecules—SNAP receptor (SNARE) and Sec1/Munc18 (SM) protein …
two classes of molecules—SNAP receptor (SNARE) and Sec1/Munc18 (SM) protein …
Munc18‐1 mutations that strongly impair SNARE‐complex binding support normal synaptic transmission
Synaptic transmission depends critically on the Sec1p/Munc18 protein Munc18‐1, but it is
unclear whether Munc18‐1 primarily operates as a integral part of the fusion machinery or …
unclear whether Munc18‐1 primarily operates as a integral part of the fusion machinery or …