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

2010 ◽  
Vol 1 (1) ◽  
Author(s):  
Jiajie Diao ◽  
Zengliu Su ◽  
Yuji Ishitsuka ◽  
Bin Lu ◽  
Kyung Suk Lee ◽  
...  
2012 ◽  
Vol 8 (1) ◽  
pp. 1-16 ◽  
Author(s):  
Minjoung Kyoung ◽  
Yunxiang Zhang ◽  
Jiajie Diao ◽  
Steven Chu ◽  
Axel T Brunger

2010 ◽  
Vol 1 (3) ◽  
pp. 168-174 ◽  
Author(s):  
Jiajie Diao ◽  
Zengliu Su ◽  
Xiaobing Lu ◽  
Tae-Young Yoon ◽  
Yeon-Kyun Shin ◽  
...  

2015 ◽  
Vol 137 (28) ◽  
pp. 8908-8911 ◽  
Author(s):  
Bokyoung Gong ◽  
Bong-Kyu Choi ◽  
Jae-Yeol Kim ◽  
Dinesh Shetty ◽  
Young Ho Ko ◽  
...  

2010 ◽  
Vol 285 (15) ◽  
pp. 11753-11753 ◽  
Author(s):  
Marta K. Domanska ◽  
Volker Kiessling ◽  
Alexander Stein ◽  
Dirk Fasshauer ◽  
Lukas K. Tamm

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Kyung Tae Kim ◽  
Yeojin Moon ◽  
Yunsu Jang ◽  
Kang Taek Lee ◽  
Changwook Lee ◽  
...  

2009 ◽  
Vol 284 (46) ◽  
pp. 32158-32166 ◽  
Author(s):  
Marta K. Domanska ◽  
Volker Kiessling ◽  
Alexander Stein ◽  
Dirk Fasshauer ◽  
Lukas K. Tamm

Author(s):  
Ryan Khounlo ◽  
Brenden J. D. Hawk ◽  
Tung-Mei Khu ◽  
Gyeongji Yoo ◽  
Nam Ki Lee ◽  
...  

SNARE-dependent membrane fusion is essential for neurotransmitter release at the synapse. Recently, α-synuclein has emerged as an important regulator for membrane fusion. Misfolded α-synuclein oligomers are potent fusion inhibitors. However, the function of normal α-synuclein has been elusive. Here, we use the single vesicle-to-supported bilayer fusion assay to dissect the role of α-synuclein in membrane fusion. The assay employs 10 kD Rhodamine B-dextran as the content probe that can detect fusion pores larger than ∼6 nm. We find that the SNARE complex alone is inefficient at dilating fusion pores. However, α-synuclein dramatically increases the probability as well as the duration of large pores. When the SNARE-interacting C-terminal region of α-synuclein was truncated, the mutant behaves the same as the wild-type. However, the double proline mutants compromising membrane-binding show significantly reduced effects on fusion pore expansion. Thus, our results suggest that α-synuclein stimulates fusion pore expansion specifically through its membrane binding.


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