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K⁺ channel gating mechanism proposed using EPR

New results indicate that a K⁺ channel switches from a closed state to an open state by widening the hydrophobic pore on the cytoplasmic side of the membrane.

Yeon-Kyun Shin
News & Views01 Jun 1998
Nature Structural Biology

Volume: 5, P: 418-420
A single-vesicle content mixing assay for SNARE-mediated membrane fusion

SNARE protein-mediated vesicle fusion is usually monitored by indirect lipid mixing. Diaoet al. have developed a FRET-based single-vesicle content mixing assay, which elucidates fusion pore formation, and shows that the yeast SNARE complex mediates pore expansion in the absence of accessory proteins.

Jiajie Diao
Zengliu Su
Taekjip Ha
Research10 Aug 2010
Nature Communications

Volume: 1, P: 1-6
Hemifusion in SNARE-mediated membrane fusion

Yibin Xu
Fan Zhang
Yeon-Kyun Shin
Research10 Apr 2005
Nature Structural & Molecular Biology

Volume: 12, P: 417-422
Synaptic vesicle fusion: today and beyond

Researchers working on synaptic vesicle fusion and neurotransmitter release share their views on the most interesting developments in their field and the challenges that lie ahead.

Nils Brose
Axel Brunger
Yongli Zhang
Special Features05 Aug 2019
Nature Structural & Molecular Biology

Volume: 26, P: 663-668
Munc18-1 induces conformational changes of syntaxin-1 in multiple intermediates for SNARE assembly

Sanghwa Lee
Jonghyeok Shin
Yeon-Kyun Shin
ResearchOpen Access15 Jul 2020
Scientific Reports

Volume: 10, P: 1-8
Synaptotagmin-1 serves as a primary Zn²⁺ sensor to mediate spontaneous neurotransmitter release under pathological conditions

In the pre-synapse, vesicle fusion is a key process for neurotransmitter release in the nervous system. Here authors demonstrate under pathological condition, synaptotagmin1 with Zn²⁺ adopts an alternative mode to regulate spontaneous neurotransmitter release.

Yijuan Xiang
Lele Cui
Ying Lai
ResearchOpen Access02 Aug 2025
Nature Communications

Volume: 16, P: 1-13
The neuronal t-SNARE complex is a parallel four-helix bundle

Wenzhong Xiao
Michelle A. Poirier
Yeon-Kyun Shin
Research01 Apr 2001
Nature Structural Biology

Volume: 8, P: 308-311
Hemifusion arrest by complexin is relieved by Ca²⁺–synaptotagmin I

Johanna R Schaub
Xiaobing Lu
James A McNew
Research16 Jul 2006
Nature Structural & Molecular Biology

Volume: 13, P: 748-750
The synaptic SNARE complex is a parallel four-stranded helical bundle

Michelle A. Poirier
Wenzhong Xiao
Mark K. Bennett
Research01 Sept 1998
Nature Structural Biology

Volume: 5, P: 765-769
Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism

Interactions between (SNARE) proteins on vesicle and target membranes provide the force necessary to drive membrane fusion. By applying piconewton forces to single SNARE complexes, the authors identify a partially assembled intermediate state that reveals how force is generated in a consistent direction.

Duyoung Min
Kipom Kim
Tae-Young Yoon
ResearchOpen Access16 Apr 2013
Nature Communications

Volume: 4, P: 1-10
Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion

The cooperative action of multiple trans SNARE complexes are a likely requirement for successful membrane fusion. New in vitro analyses reveal the kinetic timescales of the sequential steps of the fusion process, beginning with trans SNARE pairing and clustering of vesicle SNARE proteins, proceeding to hemifusion of outer bilayer leaflets, and ending with full fusion.

Xiaobing Lu
Yinghui Zhang
Yeon-Kyun Shin
Research15 Jun 2008
Nature Structural & Molecular Biology

Volume: 15, P: 700-706
Regulation of neuronal SNARE assembly by the membrane

Dae-Hyuk Kweon
Chang Sup Kim
Yeon-Kyun Shin
Research12 May 2003
Nature Structural & Molecular Biology

Volume: 10, P: 440-447
Complexin and Ca²⁺ stimulate SNARE-mediated membrane fusion

Complexin is one of several regulatory molecules known to be important for SNARE-mediated fusion that occurs during neurotransmitter release. In vitro data now suggest that complexin plays inhibitory and Ca²⁺- dependent stimulatory roles that may be correlated to changing interactions with the SNARE complex.

Tae-Young Yoon
Xiaobing Lu
Yeon-Kyun Shin
Research15 Jun 2008
Nature Structural & Molecular Biology

Volume: 15, P: 707-713
Virucidal nano-perforator of viral membrane trapping viral RNAs in the endosome

Membrane-disrupting agents that selectively target virus versus host membranes could potentially be potent antivirals. Here the authors incorporate a decoy virus receptor into a nanodisc and show that it ruptures the viral membrane at low pH and traps viral RNAs in the endolysosome for degradation.

Byoungjae Kong
Seokoh Moon
Dae-Hyuk Kweon
ResearchOpen Access14 Jan 2019
Nature Communications

Volume: 10, P: 1-10
Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump

Multidrug efflux pumps significantly contribute for bacteria resistance to antibiotics. Here the authors present the structure of Campylobacter jejuni CmeB pump combined with functional FRET assays to propose a transport mechanism where each CmeB protomers is functionally independent from the trimer.

Chih-Chia Su
Linxiang Yin
Edward W. Yu
ResearchOpen Access01 Aug 2017
Nature Communications

Volume: 8, P: 1-11
Cooperative inhibition of SNARE-mediated vesicle fusion by α-synuclein monomers and oligomers

Gyeongji Yoo
Sanghun Yeou
Nam Ki Lee
ResearchOpen Access26 May 2021
Scientific Reports

Volume: 11, P: 1-12
Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening

Ying Lai
Xiaochu Lou
Yeon-Kyun Shin
ResearchOpen Access20 Mar 2015
Scientific Reports

Volume: 5, P: 1-7
A single vesicle-vesicle fusion assay for in vitro studies of SNAREs and accessory proteins

Jiajie Diao
Yuji Ishitsuka
Taekjip Ha
Protocols19 Apr 2012
Nature Protocols

Volume: 7, P: 921-934

Search

K⁺ channel gating mechanism proposed using EPR

A single-vesicle content mixing assay for SNARE-mediated membrane fusion

Hemifusion in SNARE-mediated membrane fusion

Synaptic vesicle fusion: today and beyond

Munc18-1 induces conformational changes of syntaxin-1 in multiple intermediates for SNARE assembly

Synaptotagmin-1 serves as a primary Zn²⁺ sensor to mediate spontaneous neurotransmitter release under pathological conditions

The neuronal t-SNARE complex is a parallel four-helix bundle

Hemifusion arrest by complexin is relieved by Ca²⁺–synaptotagmin I

The synaptic SNARE complex is a parallel four-stranded helical bundle

Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism

Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion

Regulation of neuronal SNARE assembly by the membrane

Complexin and Ca²⁺ stimulate SNARE-mediated membrane fusion

Virucidal nano-perforator of viral membrane trapping viral RNAs in the endosome

Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump

Cooperative inhibition of SNARE-mediated vesicle fusion by α-synuclein monomers and oligomers

Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening

A single vesicle-vesicle fusion assay for in vitro studies of SNAREs and accessory proteins

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