Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane

Peter J. Wen, Staffan Grenklo, Gianvito Arpino, Xinyu Tan, Hsien-Shun Liao, Johanna Heureaux, Shi-Yong Peng, Hsueh-Cheng Chiang, Edaeni Hamid, Wei-Dong Zhao, Wonchul Shin, Tuomas Näreoja, Emma Evergren, Yinghui Jin, Roger Karlsson, Steven N. Ebert, Albert Jin, Allen P. Liu, Oleg Shupliakov () and Ling-Gang Wu ()
Additional contact information
Peter J. Wen: National Institute of Neurological Disorders and Stroke
Staffan Grenklo: Center of Excellence in Developmental Biology, Karolinska Institutet
Gianvito Arpino: National Institute of Neurological Disorders and Stroke
Xinyu Tan: University of Michigan
Hsien-Shun Liao: National Institute of Biomedical Imaging and Bioengineering (NIBIB)
Johanna Heureaux: University of Michigan
Shi-Yong Peng: National Institute of Neurological Disorders and Stroke
Hsueh-Cheng Chiang: National Institute of Neurological Disorders and Stroke
Edaeni Hamid: National Institute of Neurological Disorders and Stroke
Wei-Dong Zhao: National Institute of Neurological Disorders and Stroke
Wonchul Shin: National Institute of Neurological Disorders and Stroke
Tuomas Näreoja: Center of Excellence in Developmental Biology, Karolinska Institutet
Emma Evergren: Center of Excellence in Developmental Biology, Karolinska Institutet
Yinghui Jin: National Institute of Neurological Disorders and Stroke
Roger Karlsson: WGI, Stockholm University
Steven N. Ebert: Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida
Albert Jin: National Institute of Biomedical Imaging and Bioengineering (NIBIB)
Allen P. Liu: University of Michigan
Oleg Shupliakov: Center of Excellence in Developmental Biology, Karolinska Institutet
Ling-Gang Wu: National Institute of Neurological Disorders and Stroke

Nature Communications, 2016, vol. 7, issue 1, 1-14

Abstract: Abstract Vesicle fusion is executed via formation of an Ω-shaped structure (Ω-profile), followed by closure (kiss-and-run) or merging of the Ω-profile into the plasma membrane (full fusion). Although Ω-profile closure limits release but recycles vesicles economically, Ω-profile merging facilitates release but couples to classical endocytosis for recycling. Despite its crucial role in determining exocytosis/endocytosis modes, how Ω-profile merging is mediated is poorly understood in endocrine cells and neurons containing small ∼30–300 nm vesicles. Here, using confocal and super-resolution STED imaging, force measurements, pharmacology and gene knockout, we show that dynamic assembly of filamentous actin, involving ATP hydrolysis, N-WASP and formin, mediates Ω-profile merging by providing sufficient plasma membrane tension to shrink the Ω-profile in neuroendocrine chromaffin cells containing ∼300 nm vesicles. Actin-directed compounds also induce Ω-profile accumulation at lamprey synaptic active zones, suggesting that actin may mediate Ω-profile merging at synapses. These results uncover molecular and biophysical mechanisms underlying Ω-profile merging.

Date: 2016
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DOI: 10.1038/ncomms12604

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