scholarly journals Single-Vesicle Fusion Assay Reveals Munc18-1 Binding to the SNARE Core Is Sufficient for Stimulating Membrane Fusion

2010 ◽  
Vol 1 (3) ◽  
pp. 168-174 ◽  
Author(s):  
Jiajie Diao ◽  
Zengliu Su ◽  
Xiaobing Lu ◽  
Tae-Young Yoon ◽  
Yeon-Kyun Shin ◽  
...  
2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Kyung Tae Kim ◽  
Yeojin Moon ◽  
Yunsu Jang ◽  
Kang Taek Lee ◽  
Changwook Lee ◽  
...  

2012 ◽  
Vol 8 (1) ◽  
pp. 1-16 ◽  
Author(s):  
Minjoung Kyoung ◽  
Yunxiang Zhang ◽  
Jiajie Diao ◽  
Steven Chu ◽  
Axel T Brunger

2010 ◽  
Vol 107 (8) ◽  
pp. 3517-3521 ◽  
Author(s):  
Erdem Karatekin ◽  
Jérôme Di Giovanni ◽  
Cécile Iborra ◽  
Jeff Coleman ◽  
Ben O'Shaughnessy ◽  
...  

2017 ◽  
Vol 113 (11) ◽  
pp. 2573-2574 ◽  
Author(s):  
Jan W. Kuhlmann ◽  
Meike Junius ◽  
Ulf Diederichsen ◽  
Claudia Steinem

Langmuir ◽  
2018 ◽  
Vol 34 (20) ◽  
pp. 5849-5859 ◽  
Author(s):  
Sathish Ramakrishnan ◽  
Andrea Gohlke ◽  
Feng Li ◽  
Jeff Coleman ◽  
Weiming Xu ◽  
...  

2012 ◽  
Vol 7 (5) ◽  
pp. 921-934 ◽  
Author(s):  
Jiajie Diao ◽  
Yuji Ishitsuka ◽  
Hanki Lee ◽  
Chirlmin Joo ◽  
Zengliu Su ◽  
...  

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Madhurima Dhara ◽  
Antonio Yarzagaray ◽  
Mazen Makke ◽  
Barbara Schindeldecker ◽  
Yvonne Schwarz ◽  
...  

Vesicle fusion is mediated by an assembly of SNARE proteins between opposing membranes, but it is unknown whether transmembrane domains (TMDs) of SNARE proteins serve mechanistic functions that go beyond passive anchoring of the force-generating SNAREpin to the fusing membranes. Here, we show that conformational flexibility of synaptobrevin-2 TMD is essential for efficient Ca2+-triggered exocytosis and actively promotes membrane fusion as well as fusion pore expansion. Specifically, the introduction of helix-stabilizing leucine residues within the TMD region spanning the vesicle’s outer leaflet strongly impairs exocytosis and decelerates fusion pore dilation. In contrast, increasing the number of helix-destabilizing, ß-branched valine or isoleucine residues within the TMD restores normal secretion but accelerates fusion pore expansion beyond the rate found for the wildtype protein. These observations provide evidence that the synaptobrevin-2 TMD catalyzes the fusion process by its structural flexibility, actively setting the pace of fusion pore expansion.


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